Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489).
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 63(Pt 3): 168-72, 2007 Mar 01.
Article
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| MEDLINE
| ID: mdl-17329806
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Bacillus anthracis
/
Proteínas Bacterianas
/
Ligasas de Carbono-Nitrógeno
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Año:
2007
Tipo del documento:
Article
País de afiliación:
Reino Unido
Pais de publicación:
Reino Unido