Crystallization and preliminary X-ray analysis of the ergothioneine-biosynthetic methyltransferase EgtD.

2.50
Hdl Handle:
http://hdl.handle.net/10033/326009
Title:
Crystallization and preliminary X-ray analysis of the ergothioneine-biosynthetic methyltransferase EgtD.
Authors:
Vit, Allegra; Misson, Laëtitia; Blankenfeldt, Wulf ( 0000-0001-9886-9668 ) ; Seebeck, Florian Peter
Abstract:
Ergothioneine is an amino-acid betaine derivative of histidine that was discovered more than one century ago. Despite significant research pointing to a function in oxidative stress defence, the exact mechanisms of action of ergothioneine remain elusive. Although both humans and bacterial pathogens such as Mycobacterium tuberculosis seem to depend on ergothioneine, humans are devoid of the corresponding biosynthetic enzymes. Therefore, its biosynthesis may emerge as potential drug target in the development of novel therapeutics against tuberculosis. The recent identification of ergothioneine-biosynthetic genes in M. smegmatis enables a more systematic study of its biology. The pathway is initiated by EgtD, a SAM-dependent methyltransferase that catalyzes a trimethylation reaction of histidine to give N(α),N(α),N(α)-trimethylhistidine. Here, the recombinant production, purification and crystallization of EgtD are reported. Crystals of native EgtD diffracted to 2.35 Å resolution at a synchrotron beamline, whereas crystals of seleno-L-methionine-labelled protein diffracted to 1.75 Å resolution and produced a significant anomalous signal to 2.77 Å resolution at the K edge. All of the crystals belonged to space group P212121, with two EgtD monomers in the asymmetric unit.
Affiliation:
Dept of structure and functions of proteins, Hemholtz Centre for infection research, Inhoffenstr. 7, D-38124 Braunschweig, Germany.
Citation:
Crystallization and preliminary X-ray analysis of the ergothioneine-biosynthetic methyltransferase EgtD. 2014, 70 (Pt 5):676-80 Acta Crystallogr F Struct Biol Commun
Journal:
Acta crystallographica. Section F, Structural biology communications
Issue Date:
May-2014
URI:
http://hdl.handle.net/10033/326009
DOI:
10.1107/S2053230X1400805X
PubMed ID:
24817736
Type:
Article
Language:
en
ISSN:
2053-230X
Appears in Collections:
Publications of the Dept. Structure and Functions of Proteins(SFPR)

Full metadata record

DC FieldValue Language
dc.contributor.authorVit, Allegraen
dc.contributor.authorMisson, Laëtitiaen
dc.contributor.authorBlankenfeldt, Wulfen
dc.contributor.authorSeebeck, Florian Peteren
dc.date.accessioned2014-09-09T13:48:46Zen
dc.date.available2014-09-09T13:48:46Zen
dc.date.issued2014-05en
dc.identifier.citationCrystallization and preliminary X-ray analysis of the ergothioneine-biosynthetic methyltransferase EgtD. 2014, 70 (Pt 5):676-80 Acta Crystallogr F Struct Biol Communen
dc.identifier.issn2053-230Xen
dc.identifier.pmid24817736en
dc.identifier.doi10.1107/S2053230X1400805Xen
dc.identifier.urihttp://hdl.handle.net/10033/326009en
dc.description.abstractErgothioneine is an amino-acid betaine derivative of histidine that was discovered more than one century ago. Despite significant research pointing to a function in oxidative stress defence, the exact mechanisms of action of ergothioneine remain elusive. Although both humans and bacterial pathogens such as Mycobacterium tuberculosis seem to depend on ergothioneine, humans are devoid of the corresponding biosynthetic enzymes. Therefore, its biosynthesis may emerge as potential drug target in the development of novel therapeutics against tuberculosis. The recent identification of ergothioneine-biosynthetic genes in M. smegmatis enables a more systematic study of its biology. The pathway is initiated by EgtD, a SAM-dependent methyltransferase that catalyzes a trimethylation reaction of histidine to give N(α),N(α),N(α)-trimethylhistidine. Here, the recombinant production, purification and crystallization of EgtD are reported. Crystals of native EgtD diffracted to 2.35 Å resolution at a synchrotron beamline, whereas crystals of seleno-L-methionine-labelled protein diffracted to 1.75 Å resolution and produced a significant anomalous signal to 2.77 Å resolution at the K edge. All of the crystals belonged to space group P212121, with two EgtD monomers in the asymmetric unit.en
dc.language.isoenen
dc.rightsArchived with thanks to Acta crystallographica. Section F, Structural biology communicationsen
dc.titleCrystallization and preliminary X-ray analysis of the ergothioneine-biosynthetic methyltransferase EgtD.en
dc.typeArticleen
dc.contributor.departmentDept of structure and functions of proteins, Hemholtz Centre for infection research, Inhoffenstr. 7, D-38124 Braunschweig, Germany.en
dc.identifier.journalActa crystallographica. Section F, Structural biology communicationsen

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