Structure of the effector-binding domain of the LysR-type transcription factor RovM from Yersinia pseudotuberculosis.

2.50
Hdl Handle:
http://hdl.handle.net/10033/140869
Title:
Structure of the effector-binding domain of the LysR-type transcription factor RovM from Yersinia pseudotuberculosis.
Authors:
Quade, Nick; Dieckmann, Marieke; Haffke, Matthias; Heroven, Ann Kathrin; Dersch, Petra; Heinz, Dirk W
Abstract:
In enteropathogenic Yersinia, the expression of several early-phase virulence factors such as invasin is tightly regulated in response to environmental cues. The responsible regulatory network is complex, involving several regulatory RNAs and proteins such as the LysR-type transcription regulator (LTTR) RovM. In this study, the crystal structure of the effector-binding domain (EBD) of RovM, the first LTTR protein described as being involved in virulence regulation, was determined at a resolution of 2.4 Å. Size-exclusion chromatography and comparison with structures of full-length LTTRs show that RovM is most likely to adopt a tetrameric arrangement with two distant DNA-binding domains (DBDs), causing the DNA to bend around it. Additionally, a cavity was detected in RovM which could bind small inducer molecules.
Affiliation:
Department of Molecular Structural Biology, Helmholtz Centre for Infection Research, D-38124 Braunschweig, Germany.
Citation:
Structure of the effector-binding domain of the LysR-type transcription factor RovM from Yersinia pseudotuberculosis. 2011, 67 (Pt 2):81-90 Acta Crystallogr. D Biol. Crystallogr.
Journal:
Acta crystallographica. Section D, Biological crystallography
Issue Date:
Feb-2011
URI:
http://hdl.handle.net/10033/140869
DOI:
10.1107/S0907444910049681
PubMed ID:
21245528
Type:
Article
Language:
en
ISSN:
1399-0047
Appears in Collections:
Publications from Division of Molekulare Struktur Biologie (MOSB)

Full metadata record

DC FieldValue Language
dc.contributor.authorQuade, Nicken
dc.contributor.authorDieckmann, Mariekeen
dc.contributor.authorHaffke, Matthiasen
dc.contributor.authorHeroven, Ann Kathrinen
dc.contributor.authorDersch, Petraen
dc.contributor.authorHeinz, Dirk Wen
dc.date.accessioned2011-08-26T14:30:15Z-
dc.date.available2011-08-26T14:30:15Z-
dc.date.issued2011-02-
dc.identifier.citationStructure of the effector-binding domain of the LysR-type transcription factor RovM from Yersinia pseudotuberculosis. 2011, 67 (Pt 2):81-90 Acta Crystallogr. D Biol. Crystallogr.en
dc.identifier.issn1399-0047-
dc.identifier.pmid21245528-
dc.identifier.doi10.1107/S0907444910049681-
dc.identifier.urihttp://hdl.handle.net/10033/140869-
dc.description.abstractIn enteropathogenic Yersinia, the expression of several early-phase virulence factors such as invasin is tightly regulated in response to environmental cues. The responsible regulatory network is complex, involving several regulatory RNAs and proteins such as the LysR-type transcription regulator (LTTR) RovM. In this study, the crystal structure of the effector-binding domain (EBD) of RovM, the first LTTR protein described as being involved in virulence regulation, was determined at a resolution of 2.4 Å. Size-exclusion chromatography and comparison with structures of full-length LTTRs show that RovM is most likely to adopt a tetrameric arrangement with two distant DNA-binding domains (DBDs), causing the DNA to bend around it. Additionally, a cavity was detected in RovM which could bind small inducer molecules.en
dc.language.isoenen
dc.subject.meshBacterial Proteinsen
dc.subject.meshCrystallography, X-Rayen
dc.subject.meshLigandsen
dc.subject.meshModels, Molecularen
dc.subject.meshProtein Structure, Quaternaryen
dc.subject.meshProtein Structure, Tertiaryen
dc.subject.meshTranscription Factorsen
dc.subject.meshYersinia pseudotuberculosisen
dc.titleStructure of the effector-binding domain of the LysR-type transcription factor RovM from Yersinia pseudotuberculosis.en
dc.typeArticleen
dc.contributor.departmentDepartment of Molecular Structural Biology, Helmholtz Centre for Infection Research, D-38124 Braunschweig, Germany.en
dc.identifier.journalActa crystallographica. Section D, Biological crystallographyen
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