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Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489).

Authors :
Meier C
Carter LG
Winter G
Owens RJ
Stuart DI
Esnouf RM
Source :
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2007 Mar 01; Vol. 63 (Pt 3), pp. 168-72. Date of Electronic Publication: 2007 Feb 23.
Publication Year :
2007

Abstract

Bacillus anthracis is a spore-forming bacterium and the causative agent of the disease anthrax. The Oxford Protein Production Facility has been targeting proteins from B. anthracis in order to develop high-throughput technologies within the Structural Proteomics in Europe project. As part of this work, the structure of 5-formyltetrahydrofolate cyclo-ligase (BA4489) has been determined by X-ray crystallography to 1.6 A resolution. The structure, solved in complex with magnesium-ion-bound ADP and phosphate, gives a detailed picture of the proposed catalytic mechanism of the enzyme. Chemical differences from other cyclo-ligase structures close to the active site that could be exploited to design specific inhibitors are also highlighted.

Details

Language :
English
ISSN :
1744-3091
Volume :
63
Issue :
Pt 3
Database :
MEDLINE
Journal :
Acta crystallographica. Section F, Structural biology and crystallization communications
Publication Type :
Academic Journal
Accession number :
17329806
Full Text :
https://doi.org/10.1107/S1744309107007221