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| | ==Crystal structure of Alanine racemase from E.faecalis complex with cycloserine== | | ==Crystal structure of Alanine racemase from E.faecalis complex with cycloserine== |
| - | <StructureSection load='3e6e' size='340' side='right' caption='[[3e6e]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='3e6e' size='340' side='right'caption='[[3e6e]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3e6e]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E6E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E6E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3e6e]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E6E FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DCS:D-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL]-N,O-CYCLOSERYLAMIDE'>DCS</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]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3e5p|3e5p]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DCS:D-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL]-N,O-CYCLOSERYLAMIDE'>DCS</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">alr, EF_0849 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1351 "Enterococcus proteiformis" Thiercelin and Jouhaud 1903])</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=3e6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e6e OCA], [https://pdbe.org/3e6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e6e RCSB], [https://www.ebi.ac.uk/pdbsum/3e6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e6e 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>
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| - | <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=3e6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e6e OCA], [http://pdbe.org/3e6e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3e6e RCSB], [http://www.ebi.ac.uk/pdbsum/3e6e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3e6e ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q837J0_ENTFA Q837J0_ENTFA]] Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.[HAMAP-Rule:MF_01201] | + | [https://www.uniprot.org/uniprot/Q837J0_ENTFA Q837J0_ENTFA] 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: Enterococcus proteiformis thiercelin and jouhaud 1903]] | + | [[Category: Enterococcus faecalis]] |
| - | [[Category: Alanine racemase]] | + | [[Category: Large Structures]] |
| - | [[Category: Hwang, K Y]] | + | [[Category: Hwang KY]] |
| - | [[Category: Lee, E H]] | + | [[Category: Lee EH]] |
| - | [[Category: Priyadarshi, A]] | + | [[Category: Priyadarshi A]] |
| - | [[Category: Sung, M W]] | + | [[Category: Sung MW]] |
| - | [[Category: Alr]]
| + | |
| - | [[Category: Isomerase]]
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| - | [[Category: Pyridoxal phosphate]]
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| - | [[Category: Scp]]
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| Structural highlights
Function
Q837J0_ENTFA 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
Alanine racemase (AlaR) is a bacterial enzyme that belongs to the fold-type III group of pyridoxal 5'-phosphate (PLP)-dependent enzymes. AlaR catalyzes the interconversion between L- and D-alanine, which is important for peptidoglycan biosynthesis. This enzyme is common in prokaryotes, but absent in eukaryotes, which makes it an attractive target for the design of new antibacterial drugs. Here, we report the crystal structures of both the apoenzyme and the d-cycloserine (DCS) complex of AlaR from the pathogenic bacterium Enterococcus faecalis v583, at a resolution of 2.5 A. DCS is a suicide inhibitor of AlaR and, as such, serves as an antimicrobial agent and has been used to treat tuberculosis and urinary tract infection-related diseases, and makes several hydrogen bonds with the conserved active site residues, Tyr44 and Ser207, respectively. The apoenzyme crystal structure of AlaR consists of three monomers in the asymmetric unit, including a polyethylene glycol molecule in the dimer interface that surrounds one of the His 293 residues and also sits close to one side of the His 293 residue in the opposite monomer. Our results provide structural insights into AlaR that may be used for the development of new antibiotics targeting the alanine racemase in pathogenic bacteria.
Structural insights into the alanine racemase from Enterococcus faecalis.,Priyadarshi A, Lee EH, Sung MW, Nam KH, Lee WH, Kim EE, Hwang KY Biochim Biophys Acta. 2009 Jul;1794(7):1030-40. Epub 2009 Mar 26. PMID:19328247[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Priyadarshi A, Lee EH, Sung MW, Nam KH, Lee WH, Kim EE, Hwang KY. Structural insights into the alanine racemase from Enterococcus faecalis. Biochim Biophys Acta. 2009 Jul;1794(7):1030-40. Epub 2009 Mar 26. PMID:19328247 doi:10.1016/j.bbapap.2009.03.006
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