2vd8

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[[Image:2vd8.jpg|left|200px]]
 
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==The crystal structure of alanine racemase from Bacillus anthracis (BA0252)==
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The line below this paragraph, containing "STRUCTURE_2vd8", creates the "Structure Box" on the page.
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<StructureSection load='2vd8' size='340' side='right'caption='[[2vd8]], [[Resolution|resolution]] 1.47&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2vd8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis_str._Ames Bacillus anthracis str. Ames]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VD8 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.47&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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{{STRUCTURE_2vd8| PDB=2vd8 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vd8 OCA], [https://pdbe.org/2vd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vd8 RCSB], [https://www.ebi.ac.uk/pdbsum/2vd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vd8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A6L7HC45_BACAN A0A6L7HC45_BACAN] Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.[HAMAP-Rule:MF_01201]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vd/2vd8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vd8 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''THE CRYSTAL STRUCTURE OF ALANINE RACEMASE FROM BACILLUS ANTHRACIS (BA0252)'''
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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<ref>PMID:18453697</ref>
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==Overview==
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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.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2VD8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VD8 OCA].
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</div>
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<div class="pdbe-citations 2vd8" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/18453697 18453697]
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*[[Alanine racemase 3D structures|Alanine racemase 3D structures]]
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[[Category: Alanine racemase]]
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== References ==
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[[Category: Bacillus anthracis]]
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<references/>
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[[Category: Single protein]]
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__TOC__
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[[Category: Au, K.]]
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</StructureSection>
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[[Category: Esnouf, R M.]]
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[[Category: Bacillus anthracis str. Ames]]
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[[Category: Harlos, K.]]
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[[Category: Large Structures]]
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[[Category: Nettleship, J E.]]
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[[Category: Au K]]
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[[Category: Oppf, Oxford Protein Production Facility.]]
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[[Category: Esnouf RM]]
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[[Category: Owens, R J.]]
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[[Category: Harlos K]]
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[[Category: Ren, J.]]
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[[Category: Nettleship JE]]
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[[Category: Spine, Structural Proteomics in Europe.]]
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[[Category: Owens RJ]]
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[[Category: Stuart, D I.]]
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[[Category: Ren J]]
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[[Category: Walter, T S.]]
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[[Category: Stuart DI]]
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[[Category: Alanine racemase]]
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[[Category: Walter TS]]
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[[Category: D- alanine]]
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[[Category: Isomerase]]
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[[Category: L-alanine]]
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[[Category: Oppf]]
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[[Category: Oxford protein production facility]]
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[[Category: Peptidoglycan synthesis]]
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[[Category: Plp]]
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[[Category: Pyridoxal 5'-phosphate]]
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[[Category: Pyridoxal phosphate]]
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[[Category: Spore germination]]
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[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 21:38:26 2008''
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Current revision

The crystal structure of alanine racemase from Bacillus anthracis (BA0252)

PDB ID 2vd8

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