2vd9: Difference between revisions
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[[Category: Alanine racemase]] | [[Category: Alanine racemase]] | ||
[[Category: Bacillus anthracis]] | [[Category: Bacillus anthracis]] | ||
[[Category: Au, K | [[Category: Au, K]] | ||
[[Category: Esnouf, R M | [[Category: Esnouf, R M]] | ||
[[Category: Harlos, K | [[Category: Harlos, K]] | ||
[[Category: Nettleship, J E | [[Category: Nettleship, J E]] | ||
[[Category: Oppf, Oxford Protein Production Facility | [[Category: Oppf, Oxford Protein Production Facility]] | ||
[[Category: Owens, R J | [[Category: Owens, R J]] | ||
[[Category: Ren, J | [[Category: Ren, J]] | ||
[[Category: Spine, Structural Proteomics in Europe | [[Category: Spine, Structural Proteomics in Europe]] | ||
[[Category: Stuart, D I | [[Category: Stuart, D I]] | ||
[[Category: Walter, T S | [[Category: Walter, T S]] | ||
[[Category: D-alanine]] | [[Category: D-alanine]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] |
Revision as of 18:30, 19 January 2015
The crystal structure of alanine racemase from Bacillus anthracis (BA0252) with bound L-Ala-PThe crystal structure of alanine racemase from Bacillus anthracis (BA0252) with bound L-Ala-P
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBacillus 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. Structures of an alanine racemase from Bacillus anthracis (BA0252) in the presence and absence of (R)-1-aminoethylphosphonic acid (L-Ala-P).,Au K, Ren J, Walter TS, Harlos K, Nettleship JE, Owens RJ, Stuart DI, Esnouf RM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt, 5):327-33. Epub 2008 Apr 5. PMID:18453697[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Alanine racemase
- Bacillus anthracis
- Au, K
- Esnouf, R M
- Harlos, K
- Nettleship, J E
- Oppf, Oxford Protein Production Facility
- Owens, R J
- Ren, J
- Spine, Structural Proteomics in Europe
- Stuart, D I
- Walter, T S
- D-alanine
- Isomerase
- L-alanine
- Oppf
- Oxford protein production facility
- Peptidoglycan synthesis
- Plp
- Pyridoxal 5'-phosphate
- Pyridoxal phosphate
- Spore germination
- Structural genomic