2JCB
The crystal structure of 5-formyl-tetrahydrofolate cycloligase from Bacillus anthracis (BA4489)
Summary for 2JCB
| Entry DOI | 10.2210/pdb2jcb/pdb |
| Descriptor | 5-FORMYLTETRAHYDROFOLATE CYCLO-LIGASE FAMILY PROTEIN, ADENOSINE-5'-DIPHOSPHATE, PHOSPHATE ION, ... (5 entities in total) |
| Functional Keywords | ligase, folate metabolism |
| Biological source | BACILLUS ANTHRACIS |
| Total number of polymer chains | 2 |
| Total formula weight | 47936.54 |
| Authors | 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) (deposition date: 2006-12-21, release date: 2007-02-20, Last modification date: 2023-12-13) |
| Primary citation | 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 Cited by 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: 17329806DOI: 10.1107/S1744309107007221 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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