2VD8: The Crystal Structure Of Alanine Racemase From Bacillus Anthracis (ba0252)

Citation:
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.
PDB ID: 2VD8Download
MMDB ID: 64508
PDB Deposition Date: 2007/10/1
Updated in MMDB: 2015/05
Experimental Method:
x-ray diffraction
Resolution: 1.47  Å
Source Organism:
Similar Structures:
Biological Unit for 2VD8: dimeric; determined by author and by software (PQS)
Molecular Components in 2VD8
Label Count Molecule
Proteins (2 molecules)
2
Alanine Racemase
Molecule annotation
Chemicals (9 molecules)
1
2
2
4
3
3
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.