2JCB

The crystal structure of 5-formyl-tetrahydrofolate cycloligase from Bacillus anthracis (BA4489)

2JCB の概要

• エントリーDOI: 10.2210/pdb2jcb/pdb
• 分子名称: 5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE FAMILY PROTEIN, ADENOSINE-5'-DIPHOSPHATE, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: ligase, folate metabolism
• 由来する生物種: BACILLUS ANTHRACIS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47936.54

構造登録者

Meier, C.,Carter, L.G.,Winter, G.,Owens, R.J.,Stuart, D.I.,Esnouf, R.M.,Oxford Protein Production Facility (OPPF),Structural Proteomics in Europe (SPINE) (登録日: 2006-12-21, 公開日: 2007-02-20, 最終更新日: 2023-12-13)

主引用文献

Meier, C.,Carter, L.G.,Winter, G.,Owens, R.J.,Stuart, D.I.,Esnouf, R.M.
Structure of 5-Formyltetrahydrofolate Cyclo-Ligase from Bacillus Anthracis (Ba4489).
Acta Crystallogr.,Sect.F, 63:168-, 2007

PubMed 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.

PubMed: 17329806
DOI: 10.1107/S1744309107007221

実験手法

X-RAY DIFFRACTION (1.6 Å)