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

Abstract

The structure of 5-formyltetrahydrofolate cyclo-ligase from B. anthracis determined by X-ray crystallography at a resolution of 1.6 Å is described. 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.

Authors:
 [1];  [2];  [1];  [3];  [1]; ;  [1];  [2]
  1. Oxford Protein Production Facility, The Henry Wellcome Building for Genomic Medicine, Oxford University, Roosevelt Drive, Oxford OX3 7BN (United Kingdom)
  2. (United Kingdom)
  3. CCLRC Daresbury Laboratory, Warrington, Cheshire WA4 4AD (United Kingdom)
Publication Date:
OSTI Identifier:
22360284
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 3; Other Information: PMCID: PMC2330188; PMID: 17329806; PUBLISHER-ID: gx5109; OAI: oai:pubmedcentral.nih.gov:2330188; Copyright (c) International Union of Crystallography 2007; This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLOGRAPHY; DESIGN; MAGNESIUM IONS; PHOSPHATES; RESOLUTION

Citation Formats

Meier, Christoph, Division of Structural Biology, The Henry Wellcome Building for Genomic Medicine, Oxford University, Roosevelt Drive, Oxford OX3 7BN, Carter, Lester G., Winter, Graeme, Owens, Ray J., Stuart, David I., Esnouf, Robert M., E-mail: robert@strubi.ox.ac.uk, and Division of Structural Biology, The Henry Wellcome Building for Genomic Medicine, Oxford University, Roosevelt Drive, Oxford OX3 7BN. Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489). United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107007221.
Meier, Christoph, Division of Structural Biology, The Henry Wellcome Building for Genomic Medicine, Oxford University, Roosevelt Drive, Oxford OX3 7BN, Carter, Lester G., Winter, Graeme, Owens, Ray J., Stuart, David I., Esnouf, Robert M., E-mail: robert@strubi.ox.ac.uk, & Division of Structural Biology, The Henry Wellcome Building for Genomic Medicine, Oxford University, Roosevelt Drive, Oxford OX3 7BN. Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489). United Kingdom. doi:10.1107/S1744309107007221.
Meier, Christoph, Division of Structural Biology, The Henry Wellcome Building for Genomic Medicine, Oxford University, Roosevelt Drive, Oxford OX3 7BN, Carter, Lester G., Winter, Graeme, Owens, Ray J., Stuart, David I., Esnouf, Robert M., E-mail: robert@strubi.ox.ac.uk, and Division of Structural Biology, The Henry Wellcome Building for Genomic Medicine, Oxford University, Roosevelt Drive, Oxford OX3 7BN. Thu . "Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489)". United Kingdom. doi:10.1107/S1744309107007221.
@article{osti_22360284,
title = {Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489)},
author = {Meier, Christoph and Division of Structural Biology, The Henry Wellcome Building for Genomic Medicine, Oxford University, Roosevelt Drive, Oxford OX3 7BN and Carter, Lester G. and Winter, Graeme and Owens, Ray J. and Stuart, David I. and Esnouf, Robert M., E-mail: robert@strubi.ox.ac.uk and Division of Structural Biology, The Henry Wellcome Building for Genomic Medicine, Oxford University, Roosevelt Drive, Oxford OX3 7BN},
abstractNote = {The structure of 5-formyltetrahydrofolate cyclo-ligase from B. anthracis determined by X-ray crystallography at a resolution of 1.6 Å is described. 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.},
doi = {10.1107/S1744309107007221},
journal = {Acta Crystallographica. Section F},
number = Pt 3,
volume = 63,
place = {United Kingdom},
year = {Thu Mar 01 00:00:00 EST 2007},
month = {Thu Mar 01 00:00:00 EST 2007}
}
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