4beq

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==Structure of Vibrio cholerae broad spectrum racemase double mutant R173A, N174A==
==Structure of Vibrio cholerae broad spectrum racemase double mutant R173A, N174A==
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<StructureSection load='4beq' size='340' side='right' caption='[[4beq]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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<StructureSection load='4beq' size='340' side='right'caption='[[4beq]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4beq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillo_virgola_del_koch"_trevisan_1884 "bacillo virgola del koch" trevisan 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BEQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BEQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4beq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BEQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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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]] 1.5&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4be4|4be4]], [[4be9|4be9]], [[4beu|4beu]]</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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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<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'>[https://proteopedia.org/fgij/fg.htm?mol=4beq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4beq OCA], [https://pdbe.org/4beq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4beq RCSB], [https://www.ebi.ac.uk/pdbsum/4beq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4beq ProSAT]</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=4beq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4beq OCA], [http://pdbe.org/4beq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4beq RCSB], [http://www.ebi.ac.uk/pdbsum/4beq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4beq ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ALR2_VIBCH ALR2_VIBCH]] Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids (By similarity).
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[https://www.uniprot.org/uniprot/BSR_VIBCH BSR_VIBCH] Amino-acid racemase able to utilize a broad range of substrates. Reversibly racemizes ten of the 19 natural chiral amino acids known, including both non-beta-branched aliphatic amino acids (Ala, Leu, Met, Ser, Cys, Gln and Asn) and positively charged amino acids (His, Lys and Arg). Among these substrates, is the most efficient with lysine and arginine. Is also able to catalyze the racemization of several amino acids that are not typically incorporated into proteins such as ornithine and norleucine. Is not active on negatively charged (Glu and Asp) or aromatic (Tyr, Trp and Phe) amino acids and displays minimal activity towards beta-branched aliphatic (Ile, Val and Thr) substrates (PubMed:24419381). Enables bacteria to produce and release extracellular non-canonical D-amino acids (NCDAAs) that regulate diverse cellular processes which may function as part of a cooperative strategy in vibrio communities to protect non-producing members from competing bacteria (PubMed:29446806, PubMed:29028003). D-amino acid production by BsrV provides a cue for V.cholerae to decrease peptidoglycan synthesis and to alter its cell wall via incorporation of NCDAAs into the muropeptides, in adaption to stationary phase conditions (PubMed:19762646, PubMed:29028003).<ref>PMID:19762646</ref> <ref>PMID:24419381</ref> <ref>PMID:29028003</ref> <ref>PMID:29446806</ref>
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
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*[[Alanine racemase|Alanine racemase]]
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*[[Alanine racemase 3D structures|Alanine racemase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillo virgola del koch trevisan 1884]]
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[[Category: Large Structures]]
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[[Category: Alanine racemase]]
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[[Category: Vibrio cholerae]]
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[[Category: Carrasco-Lopez, C]]
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[[Category: Carrasco-Lopez C]]
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[[Category: Hermoso, J A]]
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[[Category: Hermoso JA]]
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[[Category: Isomerase]]
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Current revision

Structure of Vibrio cholerae broad spectrum racemase double mutant R173A, N174A

PDB ID 4beq

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