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| | ==The crystal structure of alanine racemase from Bacillus anthracis (BA0252)== | | ==The crystal structure of alanine racemase from Bacillus anthracis (BA0252)== |
| - | <StructureSection load='2vd8' size='340' side='right' caption='[[2vd8]], [[Resolution|resolution]] 1.47Å' scene=''> | + | <StructureSection load='2vd8' size='340' side='right'caption='[[2vd8]], [[Resolution|resolution]] 1.47Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vd8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis_(strain_ames) Bacillus anthracis (strain 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VD8 FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.47Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr> | + | <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> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vd9|2vd9]]</td></tr>
| + | <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> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alanine_racemase Alanine racemase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.1 5.1.1.1] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vd8 OCA], [http://pdbe.org/2vd8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vd8 RCSB], [http://www.ebi.ac.uk/pdbsum/2vd8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vd8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [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] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Alanine racemase|Alanine racemase]] | + | *[[Alanine racemase 3D structures|Alanine racemase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alanine racemase]] | + | [[Category: Bacillus anthracis str. Ames]] |
| - | [[Category: Au, K]] | + | [[Category: Large Structures]] |
| - | [[Category: Esnouf, R M]] | + | [[Category: Au K]] |
| - | [[Category: Harlos, K]] | + | [[Category: Esnouf RM]] |
| - | [[Category: Nettleship, J E]] | + | [[Category: Harlos K]] |
| - | [[Category: OPPF, Oxford Protein Production Facility]] | + | [[Category: Nettleship JE]] |
| - | [[Category: Owens, R J]] | + | [[Category: Owens RJ]] |
| - | [[Category: Ren, J]] | + | [[Category: Ren J]] |
| - | [[Category: SPINE, Structural Proteomics in Europe]]
| + | [[Category: Stuart DI]] |
| - | [[Category: Stuart, D I]] | + | [[Category: Walter TS]] |
| - | [[Category: Walter, T S]] | + | |
| - | [[Category: D- alanine]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: L-alanine]]
| + | |
| - | [[Category: Oppf]]
| + | |
| - | [[Category: Oxford protein production facility]]
| + | |
| - | [[Category: Peptidoglycan synthesis]]
| + | |
| - | [[Category: Plp]]
| + | |
| - | [[Category: Pyridoxal 5'-phosphate]]
| + | |
| - | [[Category: Pyridoxal phosphate]]
| + | |
| - | [[Category: Spore germination]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| Structural highlights
Function
A0A6L7HC45_BACAN Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.[HAMAP-Rule:MF_01201]
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 PubMed
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.
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 Also
References
- ↑ Au K, Ren J, Walter TS, Harlos K, Nettleship JE, Owens RJ, Stuart DI, Esnouf RM. 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 Struct Biol Cryst Commun. 2008 May 1;64(Pt, 5):327-33. Epub 2008 Apr 5. PMID:18453697 doi:10.1107/S1744309108007252
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