2VD8
The crystal structure of alanine racemase from Bacillus anthracis (BA0252)
Summary for 2VD8
| Entry DOI | 10.2210/pdb2vd8/pdb |
| Related | 2VD9 |
| Descriptor | ALANINE RACEMASE, PYRIDOXAL-5'-PHOSPHATE, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | pyridoxal 5'-phosphate, peptidoglycan synthesis, plp, oppf, l-alanine, isomerase, d- alanine, pyridoxal phosphate, structural genomics, alanine racemase, spore germination, oxford protein production facility, structural proteomics in europe (spine) |
| Biological source | BACILLUS ANTHRACIS |
| Total number of polymer chains | 2 |
| Total formula weight | 89399.72 |
| Authors | Au, K.,Ren, J.,Walter, T.S.,Harlos, K.,Nettleship, J.E.,Owens, R.J.,Stuart, D.I.,Esnouf, R.M.,Oxford Protein Production Facility (OPPF),Structural Proteomics in Europe (SPINE) (deposition date: 2007-10-01, release date: 2008-05-20, Last modification date: 2023-12-13) |
| Primary citation | Au, K.,Ren, J.,Walter, T.S.,Harlos, K.,Nettleship, J.E.,Owens, R.J.,Stuart, D.I.,Esnouf, R.M. Structures of an Alanine Racemase from Bacillus Anthracis (Ba0252) in the Presence and Absence of (R)-1-Aminoethylphosphonic Acid (L-Ala-P). Acta Crystallogr.,Sect.F, 64:327-, 2008 Cited by PubMed Abstract: Bacillus anthracis, the causative agent of anthrax, has been targeted by the Oxford Protein Production Facility to validate high-throughput protocols within the Structural Proteomics in Europe project. As part of this work, the structures of an alanine racemase (BA0252) in the presence and absence of the inhibitor (R)-1-aminoethylphosphonic acid (L-Ala-P) have determined by X-ray crystallography to resolutions of 2.1 and 1.47 A, respectively. Difficulties in crystallizing this protein were overcome by the use of reductive methylation. Alanine racemase has attracted much interest as a possible target for anti-anthrax drugs: not only is D-alanine a vital component of the bacterial cell wall, but recent studies also indicate that alanine racemase, which is accessible in the exosporium, plays a key role in inhibition of germination in B. anthracis. These structures confirm the binding mode of L-Ala-P but suggest an unexpected mechanism of inhibition of alanine racemase by this compound and could provide a basis for the design of improved alanine racemase inhibitors with potential as anti-anthrax therapies. PubMed: 18453697DOI: 10.1107/S1744309108007252 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.47 Å) |
Structure validation
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