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

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 wo...

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Detalles Bibliográficos
Autores principales: Meier, Christoph, Carter, Lester G., Winter, Graeme, Owens, Ray J., Stuart, David I., Esnouf, Robert M.
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2330188/
https://www.ncbi.nlm.nih.gov/pubmed/17329806
http://dx.doi.org/10.1107/S1744309107007221
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author Meier, Christoph
Carter, Lester G.
Winter, Graeme
Owens, Ray J.
Stuart, David I.
Esnouf, Robert M.
author_facet Meier, Christoph
Carter, Lester G.
Winter, Graeme
Owens, Ray J.
Stuart, David I.
Esnouf, Robert M.
author_sort Meier, Christoph
collection PubMed
description 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 Å 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.
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spelling pubmed-23301882008-05-12 Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489) Meier, Christoph Carter, Lester G. Winter, Graeme Owens, Ray J. Stuart, David I. Esnouf, Robert M. Acta Crystallogr Sect F Struct Biol Cryst Commun Protein Structure Communications 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 Å 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. International Union of Crystallography 2007-02-23 /pmc/articles/PMC2330188/ /pubmed/17329806 http://dx.doi.org/10.1107/S1744309107007221 Text en © International Union of Crystallography 2007 http://journals.iucr.org/services/termsofuse.html This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html.
spellingShingle Protein Structure Communications
Meier, Christoph
Carter, Lester G.
Winter, Graeme
Owens, Ray J.
Stuart, David I.
Esnouf, Robert M.
Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489)
title Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489)
title_full Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489)
title_fullStr Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489)
title_full_unstemmed Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489)
title_short Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489)
title_sort structure of 5-formyltetrahydrofolate cyclo-ligase from bacillus anthracis (ba4489)
topic Protein Structure Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2330188/
https://www.ncbi.nlm.nih.gov/pubmed/17329806
http://dx.doi.org/10.1107/S1744309107007221
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