2024-03-28T10:04:18Zhttp://repository.helmholtz-hzi.de/oai/requestoai:repository.helmholtz-hzi.de:10033/3018082019-08-30T11:34:48Zcom_10033_311308col_10033_620561
Helmholtz Zentrum für Infektionsforschung Repository
author
Hofmeyer, Thomas
author
Schmelz, Stefan
author
Degiacomi, Matteo T
author
Dal Peraro, Matteo
author
Daneschdar, Matin
author
Scrima, Andrea
author
van den Heuvel, Joop
author
Heinz, Dirk W
author
Kolmar, Harald
department
Institute for Organic Chemistry and Biochemistry, Technische Universität Darmstadt, Petersenstraße 22, 64287 Darmstadt, Germany.
2013-09-18T14:16:21Z
2013-04-26
Arranged sevenfold: structural insights into the C-terminal oligomerization domain of human C4b-binding protein. 2013, 425 (8):1302-17 J. Mol. Biol.
1089-8638
23274142
10.1016/j.jmb.2012.12.017
http://hdl.handle.net/10033/301808
Journal of molecular biology
The complement system as a major part of innate immunity is the first line of defense against invading microorganisms. Orchestrated by more than 60 proteins, its major task is to discriminate between host cells and pathogens and to initiate immune response. Additional recognition of necrotic or apoptotic cells demands a fine-tune regulation of this powerful system. C4b-binding protein (C4BP) is the major inhibitor of the classical complement and lectin pathway. The crystal structure of the human C4BP oligomerization domain in its 7α isoform and molecular simulations provide first structural insights of C4BP oligomerization. The heptameric core structure is stabilized by intermolecular disulfide bonds. In addition, thermal shift assays indicate that layers of electrostatic interactions mainly contribute to the extraordinary thermodynamic stability of the complex. These findings make C4BP a promising scaffold for multivalent ligand display with applications in immunology and biological chemistry.
en
Archived with thanks to Journal of molecular biology
Arranged sevenfold: structural insights into the C-terminal oligomerization domain of human C4b-binding protein.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/301808/1/Hofmeyer%20et%20al_final.pdf
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Hofmeyer et al 2013 supplemental.pdf.txt
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oai:repository.helmholtz-hzi.de:10033/6207832018-06-13T00:40:48Zcom_10033_311308col_10033_620561
Helmholtz Zentrum für Infektionsforschung Repository
author
He, Feng Q
author
Sauermann, Ulrike
author
Beer, Christiane
author
Winkelmann, Silke
author
Yu, Zheng
author
Sopper, Sieghart
author
Zeng, An-Ping
author
Wirth, Manfred
2017-01-27T11:36:19Z
2014-08-27
Virology Journal. 2014 Aug 27;11(1):152
http://dx.doi.org/10.1186/1743-422X-11-152
Abstract Background The deciphering of cellular networks to determine susceptibility to infection by HIV or the related simian immunodeficiency virus (SIV) is a major challenge in infection biology. Results Here, we have compared gene expression profiles of a human CD4+ T cell line at 24 h after infection with a cell line of the same origin permanently releasing SIVmac. A new knowledge-based-network approach (Inter-Chain-Finder, ICF) has been used to identify sub-networks associated with cell survival of a chronically SIV-infected T cell line. Notably, the method can identify not only differentially expressed key hub genes but also non-differentially expressed, critical, ‘hidden’ regulators. Six out of the 13 predicted major hidden key regulators were among the landscape of proteins known to interact with HIV. Several sub-networks were dysregulated upon chronic infection with SIV. Most prominently, factors reported to be engaged in early stages of acute viral infection were affected, e.g. entry, integration and provirus transcription and other cellular responses such as apoptosis and proliferation were modulated. For experimental validation of the gene expression analyses and computational predictions, individual pathways/sub-networks and significantly altered key regulators were investigated further. We showed that the expression of caveolin-1 (Cav-1), the top hub in the affected protein-protein interaction network, was significantly upregulated in chronically SIV-infected CD4+ T cells. Cav-1 is the main determinant of caveolae and a central component of several signal transduction pathways. Furthermore, CD4 downregulation and modulation of the expression of alternate and co-receptors as well as pathways associated with viral integration into the genome were also observed in these cells. Putatively, these modifications interfere with re-infection and the early replication cycle and inhibit cell death provoked by syncytia formation and bystander apoptosis. Conclusions Thus, by using the novel approach for network analysis, ICF, we predict that in the T cell line chronically infected with SIV, cellular processes that are known to be crucial for early phases of HIV/SIV replication are altered and cellular responses that result in cell death are modulated. These modifications presumably contribute to cell survival despite chronic infection.
en
Identification of molecular sub-networks associated with cell survival in a chronically SIVmac-infected human CD4+ T cell line
Journal Article
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https://hzi.openrepository.com/bitstream/10033/620783/1/12985_2013_Article_2486.pdf
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oai:repository.helmholtz-hzi.de:10033/6206042019-08-30T11:31:23Zcom_10033_311308col_10033_620561
Helmholtz Zentrum für Infektionsforschung Repository
author
Moes, Lorin
author
Wirth, Manfred
2016-11-29T08:51:06Z
2007-11-22
The internal initiation of translation in bovine viral diarrhea virus RNA depends on the presence of an RNA pseudoknot upstream of the initiation codon. 2007, 4:124 Virol. J.
1743-422X
18034871
10.1186/1743-422X-4-124
http://hdl.handle.net/10033/620604
Virology journal
Bovine viral diarrhea virus (BVDV) is the prototype representative of the pestivirus genus in the Flaviviridae family. It has been shown that the initiation of translation of BVDV RNA occurs by an internal ribosome entry mechanism mediated by the 5' untranslated region of the viral RNA 1. The 5' and 3' boundaries of the IRES of the cytopathic BVDV NADL have been mapped and it has been suggested that the IRES extends into the coding of the BVDV polyprotein 2. A putative pseudoknot structure has been recognized in the BVDV 5'UTR in close proximity to the AUG start codon. A pseudoknot structure is characteristic for flavivirus IRESes and in the case of the closely related classical swine fever virus (CSFV) and the more distantly related Hepatitis C virus (HCV) pseudoknot function in translation has been demonstrated.
Archived with thanks to Virology journal
The internal initiation of translation in bovine viral diarrhea virus RNA depends on the presence of an RNA pseudoknot upstream of the initiation codon.
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oai:repository.helmholtz-hzi.de:10033/6206882019-08-30T11:33:57Zcom_10033_311308com_10033_620618col_10033_620619col_10033_559591col_10033_620561
Helmholtz Zentrum für Infektionsforschung Repository
author
Bock, Tobias
author
Volz, Carsten
author
Hering, Vanessa
author
Scrima, Andrea
author
Müller, Rolf
author
Blankenfeldt, Wulf
department
Hel,holtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany.
2017-01-09T15:31:16Z
2016-12-09
The AibR-isovaleryl coenzyme A regulator and its DNA binding site - a model for the regulation of alternative de novo isovaleryl coenzyme A biosynthesis in Myxococcus xanthus. 2016 Nucleic Acids Res.
1362-4962
27940564
10.1093/nar/gkw1238
http://hdl.handle.net/10033/620688
Nucleic acids research
Isovaleryl coenzyme A (IV-CoA) is an important building block of iso-fatty acids. In myxobacteria, IV-CoA is essential for the formation of signaling molecules involved in fruiting body formation. Leucine degradation is the common source of IV-CoA, but a second, de novo biosynthetic route to IV-CoA termed AIB (alternative IV-CoA biosynthesis) was recently discovered in M. xanthus The AIB-operon contains the TetR-like transcriptional regulator AibR, which we characterize in this study. We demonstrate that IV-CoA binds AibR with micromolar affinity and show by gelshift experiments that AibR interacts with the promoter region of the AIB-operon once IV-CoA is present. We identify an 18-bp near-perfect palindromic repeat as containing the AibR operator and provide evidence that AibR also controls an additional genomic locus coding for a putative acetyl-CoA acetyltransferase. To elucidate atomic details, we determined crystal structures of AibR in the apo, the IV-CoA- and the IV-CoA-DNA-bound state to 1.7 Å, 2.35 Å and 2.92 Å, respectively. IV-CoA induces partial unfolding of an α-helix, which allows sequence-specific interactions between AibR and its operator. This study provides insights into AibR-mediated regulation and shows that AibR functions in an unusual TetR-like manner by blocking transcription not in the ligand-free but in the effector-bound state.
en
The AibR-isovaleryl coenzyme A regulator and its DNA binding site - a model for the regulation of alternative de novo isovaleryl coenzyme A biosynthesis in Myxococcus xanthus.
Article
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URL
https://hzi.openrepository.com/bitstream/10033/620688/1/Bock%20et%20al.pdf
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oai:repository.helmholtz-hzi.de:10033/6211002021-07-05T15:12:57Zcom_10033_311308com_10033_128109com_10033_622921col_10033_622922col_10033_621829col_10033_620561
Helmholtz Zentrum für Infektionsforschung Repository
author
Chaudhry, M Zeeshan
author
Kasmapour, Bahram
author
Plaza-Sirvent, Carlos
author
Bajagic, Milica
author
Casalegno Garduño, Rosaely
author
Borkner, Lisa
author
Lenac Roviš, Tihana
author
Scrima, Andrea
author
Jonjic, Stipan
author
Schmitz, Ingo
author
Cicin-Sain, Luka
department
Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7, 38124 Braunschweig, Germany.
2017-09-11T10:30:46Z
2017
UL36 Rescues Apoptosis Inhibition and In vivo Replication of a Chimeric MCMV Lacking the M36 Gene. 2017, 7:312 Front Cell Infect Microbiol
2235-2988
28770171
10.3389/fcimb.2017.00312
http://hdl.handle.net/10033/621100
Frontiers in cellular and infection microbiology
Apoptosis is an important defense mechanism mounted by the immune system to control virus replication. Hence, cytomegaloviruses (CMV) evolved and acquired numerous anti-apoptotic genes. The product of the human CMV (HCMV) UL36 gene, pUL36 (also known as vICA), binds to pro-caspase-8, thus inhibiting death-receptor apoptosis and enabling viral replication in differentiated THP-1 cells. In vivo studies of the function of HCMV genes are severely limited due to the strict host specificity of cytomegaloviruses, but CMV orthologues that co-evolved with other species allow the experimental study of CMV biology in vivo. The mouse CMV (MCMV) homolog of the UL36 gene is called M36, and its protein product (pM36) is a functional homolog of vICA that binds to murine caspase-8 and inhibits its activation. M36-deficient MCMV is severely growth impaired in macrophages and in vivo. Here we show that pUL36 binds to the murine pro-caspase-8, and that UL36 expression inhibits death-receptor apoptosis in murine cells and can replace M36 to allow MCMV growth in vitro and in vivo. We generated a chimeric MCMV expressing the UL36 ORF sequence instead of the M36 one. The newly generated MCMV(UL36) inhibited apoptosis in macrophage lines RAW 264.7, J774A.1, and IC-21 and its growth was rescued to wild type levels. Similarly, growth was rescued in vivo in the liver and spleen, but only partially in the salivary glands of BALB/c and C57BL/6 mice. In conclusion, we determined that an immune-evasive HCMV gene is conserved enough to functionally replace its MCMV counterpart and thus allow its study in an in vivo setting. As UL36 and M36 proteins engage the same molecular host target, our newly developed model can facilitate studies of anti-viral compounds targeting pUL36 in vivo.
en
UL36 Rescues Apoptosis Inhibition and In vivo Replication of a Chimeric MCMV Lacking the M36 Gene.
Article
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URL
https://repository.helmholtz-hzi.de/bitstream/10033/621100/1/Chaudhry%20et%20al.pdf
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oai:repository.helmholtz-hzi.de:10033/6211572019-08-30T11:27:16Zcom_10033_311308col_10033_620561
Helmholtz Zentrum für Infektionsforschung Repository
author
Archna, Archna
author
Scrima, Andrea
department
Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr.7, 38124 Braunschweig, Germany.
2017-11-03T10:13:04Z
2017-10-01
Identification, biochemical characterization and crystallization of the central region of human ATG16L1. 2017, 73 (Pt 10):560-567 Acta Crystallogr F Struct Biol Commun
2053-230X
28994404
10.1107/S2053230X17013280
http://hdl.handle.net/10033/621157
Acta crystallographica. Section F, Structural biology communications
ATG16L1 plays a major role in autophagy. It acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. The ATG12~ATG5-ATG16L1 complex is one of the key complexes involved in autophagosome formation. Human ATG16L1 comprises 607 amino acids with three functional domains named ATG5BD, CCD and WD40, where the C-terminal WD40 domain represents approximately 50% of the full-length protein. Previously, structures of the C-terminal WD40 domain of human ATG16L1 as well as of human ATG12~ATG5 in complex with the ATG5BD of ATG16L1 have been reported. However, apart from the ATG5BD, no structural information for the N-terminal half, including the CCD, of human ATG16L1 is available. In this study, the authors aimed to structurally characterize the N-terminal half of ATG16L1. ATG16L111-307 in complex with ATG5 has been purified and crystallized in two crystal forms. However, both crystal structures revealed degradation of ATG16L1, resulting in crystals comprising only full-length ATG5 and the ATG5BD of ATG16L1. The structures of ATG5-ATG5BD in two novel crystal forms are presented, further supporting the previously observed dimerization of ATG5-ATG16L1. The reported degradation points towards a high instability at the linker region between the ATG5BD and the CCD in ATG16L1. Based on this observation and further biochemical analysis of ATG16L1, a stable 236-amino-acid subfragment comprising residues 72-307 of the N-terminal half of ATG16L1, covering the residual, so far structurally uncharacterized region of human ATG16L1, was identified. Here, the identification, purification, biochemical characterization and crystallization of the proteolytically stable ATG16L172-307 subfragment are reported.
en
Identification, biochemical characterization and crystallization of the central region of human ATG16L1.
Article
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oai:repository.helmholtz-hzi.de:10033/6213212019-08-30T11:29:17Zcom_10033_311308col_10033_620561
Helmholtz Zentrum für Infektionsforschung Repository
author
Fiebig, David
author
Schmelz, Stefan
author
Zindel, Stephan
author
Ehret, Vera
author
Beck, Jan
author
Ebenig, Aileen
author
Ehret, Marina
author
Fröls, Sabrina
author
Pfeifer, Felicitas
author
Kolmar, Harald
author
Fuchsbauer, Hans-Lothar
author
Scrima, Andrea
department
Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7, 38124 Braunschweig, Germany.
2018-03-12T15:28:28Z
2016
Structure of the Dispase Autolysis-inducing Protein from Streptomyces mobaraensis and Glutamine Cross-linking Sites for Transglutaminase. 2016, 291 (39):20417-26 J. Biol. Chem.
1083-351X
27493205
10.1074/jbc.M116.731109
http://hdl.handle.net/10033/621321
The Journal of biological chemistry
PMC5034039
Transglutaminase from Streptomyces mobaraensis (MTG) is an important enzyme for cross-linking and modifying proteins. An intrinsic substrate of MTG is the dispase autolysis-inducing protein (DAIP). The amino acid sequence of DAIP contains 5 potential glutamines and 10 lysines for MTG-mediated cross-linking. The aim of the study was to determine the structure and glutamine cross-linking sites of the first physiological MTG substrate. A production procedure was established in Escherichia coli BL21 (DE3) to obtain high yields of recombinant DAIP. DAIP variants were prepared by replacing four of five glutamines for asparagines in various combinations via site-directed mutagenesis. Incorporation of biotin cadaverine revealed a preference of MTG for the DAIP glutamines in the order of Gln-39 ≫ Gln-298 > Gln-345 ∼ Gln-65 ≫ Gln-144. In the structure of DAIP the preferred glutamines do cluster at the top of the seven-bladed β-propeller. This suggests a targeted cross-linking of DAIP by MTG that may occur after self-assembly in the bacterial cell wall. Based on our biochemical and structural data of the first physiological MTG substrate, we further provide novel insight into determinants of MTG-mediated modification, specificity, and efficiency.
en
Structure of the Dispase Autolysis-inducing Protein from Streptomyces mobaraensis and Glutamine Cross-linking Sites for Transglutaminase.
Article
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oai:repository.helmholtz-hzi.de:10033/6213322019-08-30T11:29:17Zcom_10033_128109com_10033_620644com_10033_311308col_10033_128110col_10033_620646col_10033_620561
Helmholtz Zentrum für Infektionsforschung Repository
author
Sadana, Pooja
author
Geyer, Rebecca
author
Pezoldt, Joern
author
Helmsing, Saskia
author
Huehn, Jochen
author
Hust, Michael
author
Dersch, Petra
author
Scrima, Andrea
department
Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7, 38124 Braunschweig, Germany.
2018-03-23T15:04:02Z
2018-03-13
The invasin D protein fromYersinia pseudotuberculosisselectively binds the Fab region of host antibodies and affects colonization of the intestine. 2018 J. Biol. Chem.
1083-351X
29535184
10.1074/jbc.RA117.001068
http://hdl.handle.net/10033/621332
The Journal of biological chemistry
Yersinia pseudotuberculosis is a Gram-negative bacterium and zoonotic pathogen responsible for a wide range of diseases, ranging from mild diarrhea, enterocolitis, lymphatic adenitis to persistent local inflammation. TheY. pseudotuberculosisinvasin D (InvD) molecule belongs to the invasin (InvA)-type autotransporter proteins, but its structure and function remain unknown. In this study, we present the first crystal structure of InvD, analyzed its expression and function in a murine infection model, and identified its target molecule in the host. We found that InvD is induced at 37°C and expressed in vivo2-4 days after infection, indicating that InvD is a virulence factor. During infection, InvD was expressed in all parts of the intestinal tract, but not in deeper lymphoid tissues. The crystal structure of the C-terminal adhesion domain of InvD revealed a distinct Ig-related fold, that, apart from the canonical β-sheets, comprises various modifications of and insertions into the Ig-core structure. We identified the Fab fragment of host-derived IgG/IgA antibodies as the target of the adhesion domain. Phage display panning and flow cytometry data further revealed that InvD exhibits a preferential binding specificity toward antibodies with VH3/VK1 variable domains and that it is specifically recruited to a subset of B cells. This finding suggests that InvD modulates Ig functions in the intestine and affects direct interactions with a subset of cell surface-exposed B-cell receptors. In summary, our results provide extensive insights into the structure of InvD and its specific interaction with the target molecule in the host.
en
The invasin D protein fromYersinia pseudotuberculosisselectively binds the Fab region of host antibodies and affects colonization of the intestine.
Article
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oai:repository.helmholtz-hzi.de:10033/6219632019-10-01T07:08:45Zcom_10033_311308col_10033_559591col_10033_620561
Helmholtz Zentrum für Infektionsforschung Repository
author
Juettner, Norbert E.
author
Schmelz, Stefan
author
Anderl, Anita
author
Colin, Felix
author
Classen, Moritz
author
Pfeifer, Felicitas
author
Scrima, Andrea
author
Fuchsbauer, Hans‐Lothar
department
HZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany.
2019-09-30T12:19:06Z
2019-08-29
FEBS J. 2019 Aug 17. doi: 10.1111/febs.15044.
1742-464X
10.1111/febs.15044
http://hdl.handle.net/10033/621963
FEBS journal
Streptomyces mobaraensis is a key player for the industrial production of the protein cross-linking enzyme microbial transglutaminase (MTG). Extra-cellular activation of MTG by the transglutaminase-activating metalloprotease (TAMP) is regulated by the TAMP inhibitory protein SSTI that belongs to the large Streptomyces subtilisin inhibitor (SSI) family. Despite decades of SSI research, the binding site for metalloproteases such as TAMP remained elusive in most of the SSI proteins. Moreover, SSTI is a MTG substrate, and the preferred glutamine residues for SSTI cross-linking are not determined. To address both issues, that is, determination of the TAMP and the MTG glutamine binding sites, SSTI was modified by distinct point mutations as well as elongation or truncation of the N-terminal peptide by six and three residues respectively. Structural integrity of the mutants was verified by the determination of protein melting points and supported by unimpaired subtilisin inhibitory activity. While exchange of single amino acids could not disrupt decisively the SSTI TAMP interaction, the N-terminally shortened variants clearly indicated the highly conserved Leu40-Tyr41 as binding motif for TAMP. Moreover, enzymatic biotinylation revealed that an adjacent glutamine pair, upstream from Leu40-Tyr41 in the SSTI precursor protein, is the preferred binding site of MTG. This extension peptide disturbs the interaction with TAMP. The structure of SSTI was furthermore determined by X-ray crystallography. While no structural data could be obtained for the N-terminal peptide due to flexibility, the core structure starting from Tyr41 could be determined and analysed, which superposes well with SSI-family proteins. ENZYMES: Chymotrypsin, EC3.4.21.1; griselysin (SGMPII, SgmA), EC3.4.24.27; snapalysin (ScNP), EC3.4.24.77; streptogrisin-A (SGPA), EC3.4.21.80; streptogrisin-B (SGPB), EC3.4.21.81; subtilisin BPN', EC3.4.21.62; transglutaminase, EC2.3.2.13; transglutaminase-activating metalloprotease (TAMP), EC3.4.-.-; tri-/tetrapeptidyl aminopeptidase, EC3.4.11.-; trypsin, EC3.4.21.4. DATABASES: The atomic coordinates and structure factors (PDB 6I0I) have been deposited in the Protein Data Bank (http://www.rcsb.org).
en
Attribution-NonCommercial-ShareAlike 4.0 International
Cell Biology
Biochemistry
Molecular Biology
The N‐terminal peptide of the transglutaminase‐activating metalloprotease inhibitor from Streptomyces mobaraensis accommodates both inhibition and glutamine cross‐linking sites
Article
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oai:repository.helmholtz-hzi.de:10033/6226882021-01-29T11:12:46Zcom_10033_311308col_10033_559591col_10033_620561
Helmholtz Zentrum für Infektionsforschung Repository
author
Juettner, Norbert E
author
Schmelz, Stefan
author
Anderl, Anita
author
Colin, Felix
author
Classen, Moritz
author
Pfeifer, Felicitas
author
Scrima, Andrea
author
Fuchsbauer, Hans-Lothar
department
HZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany.
2021-01-19T11:41:53Z
2019-08-29
FEBS J. 2020 Feb;287(4):708-720. doi: 10.1111/febs.15044. Epub 2019 Aug 29.
31420998
10.1111/febs.15044
http://hdl.handle.net/10033/622688
1742-4658
The FEBS journal
Streptomyces mobaraensis is a key player for the industrial production of the protein cross-linking enzyme microbial transglutaminase (MTG). Extra-cellular activation of MTG by the transglutaminase-activating metalloprotease (TAMP) is regulated by the TAMP inhibitory protein SSTI that belongs to the large Streptomyces subtilisin inhibitor (SSI) family. Despite decades of SSI research, the binding site for metalloproteases such as TAMP remained elusive in most of the SSI proteins. Moreover, SSTI is a MTG substrate, and the preferred glutamine residues for SSTI cross-linking are not determined. To address both issues, that is, determination of the TAMP and the MTG glutamine binding sites, SSTI was modified by distinct point mutations as well as elongation or truncation of the N-terminal peptide by six and three residues respectively. Structural integrity of the mutants was verified by the determination of protein melting points and supported by unimpaired subtilisin inhibitory activity. While exchange of single amino acids could not disrupt decisively the SSTI TAMP interaction, the N-terminally shortened variants clearly indicated the highly conserved Leu40-Tyr41 as binding motif for TAMP. Moreover, enzymatic biotinylation revealed that an adjacent glutamine pair, upstream from Leu40-Tyr41 in the SSTI precursor protein, is the preferred binding site of MTG. This extension peptide disturbs the interaction with TAMP. The structure of SSTI was furthermore determined by X-ray crystallography. While no structural data could be obtained for the N-terminal peptide due to flexibility, the core structure starting from Tyr41 could be determined and analysed, which superposes well with SSI-family proteins. ENZYMES: Chymotrypsin, EC3.4.21.1; griselysin (SGMPII, SgmA), EC3.4.24.27; snapalysin (ScNP), EC3.4.24.77; streptogrisin-A (SGPA), EC3.4.21.80; streptogrisin-B (SGPB), EC3.4.21.81; subtilisin BPN', EC3.4.21.62; transglutaminase, EC2.3.2.13; transglutaminase-activating metalloprotease (TAMP), EC3.4.-.-; tri-/tetrapeptidyl aminopeptidase, EC3.4.11.-; trypsin, EC3.4.21.4. DATABASES: The atomic coordinates and structure factors (PDB 6I0I) have been deposited in the Protein Data Bank (http://www.rcsb.org).
en
Attribution 4.0 International
Streptomyces mobaraensis
crystal structure
metalloprotease inhibitor
serine protease inhibitor
transglutaminase
The N-terminal peptide of the transglutaminase-activating metalloprotease inhibitor from Streptomyces mobaraensis accommodates both inhibition and glutamine cross-linking sites.
Article
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