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| | <StructureSection load='4bf5' size='340' side='right'caption='[[4bf5]], [[Resolution|resolution]] 1.45Å' scene=''> | | <StructureSection load='4bf5' size='340' side='right'caption='[[4bf5]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4bf5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeromonas_hydrophila_subsp._hydrophila Aeromonas hydrophila subsp. hydrophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BF5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BF5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4bf5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeromonas_hydrophila_subsp._hydrophila Aeromonas hydrophila subsp. hydrophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BF5 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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]] 1.45Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4beq|4beq]], [[4beu|4beu]]</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4bf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bf5 OCA], [https://pdbe.org/4bf5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bf5 RCSB], [https://www.ebi.ac.uk/pdbsum/4bf5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bf5 ProSAT]</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=4bf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bf5 OCA], [http://pdbe.org/4bf5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bf5 RCSB], [http://www.ebi.ac.uk/pdbsum/4bf5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bf5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0KLG5_AERHH A0KLG5_AERHH]] Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids (By similarity).[HAMAP-Rule:MF_01201] | + | [https://www.uniprot.org/uniprot/BSR_AERHH BSR_AERHH] 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). 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 (By similarity).[UniProtKB:Q9KSE5]<ref>PMID:24419381</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Aeromonas hydrophila subsp. hydrophila]] | | [[Category: Aeromonas hydrophila subsp. hydrophila]] |
| - | [[Category: Alanine racemase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Carrasco-Lopez, C]] | + | [[Category: Carrasco-Lopez C]] |
| - | [[Category: Hermoso, J A]] | + | [[Category: Hermoso JA]] |
| - | [[Category: D-amino acid]]
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| - | [[Category: Isomerase]]
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| Structural highlights
Function
BSR_AERHH 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). 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 (By similarity).[UniProtKB:Q9KSE5][1]
Publication Abstract from PubMed
Broad-spectrum amino-acid racemases (Bsrs) enable bacteria to generate noncanonical D-amino acids, the roles of which in microbial physiology, including the modulation of cell-wall structure and the dissolution of biofilms, are just beginning to be appreciated. Here, extensive crystallographic, mutational, biochemical and bioinformatic studies were used to define the molecular features of the racemase BsrV that enable this enzyme to accommodate more diverse substrates than the related PLP-dependent alanine racemases. Conserved residues were identified that distinguish BsrV and a newly defined family of broad-spectrum racemases from alanine racemases, and these residues were found to be key mediators of the multispecificity of BrsV. Finally, the structural analysis of an additional Bsr that was identified in the bioinformatic analysis confirmed that the distinguishing features of BrsV are conserved among Bsr family members.
Structural basis for the broad specificity of a new family of amino-acid racemases.,Espaillat A, Carrasco-Lopez C, Bernardo-Garcia N, Pietrosemoli N, Otero LH, Alvarez L, de Pedro MA, Pazos F, Davis BM, Waldor MK, Hermoso JA, Cava F Acta Crystallogr D Biol Crystallogr. 2014 Jan;70(Pt 1):79-90. doi:, 10.1107/S1399004713024838. Epub 2013 Dec 24. PMID:24419381[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Espaillat A, Carrasco-Lopez C, Bernardo-Garcia N, Pietrosemoli N, Otero LH, Alvarez L, de Pedro MA, Pazos F, Davis BM, Waldor MK, Hermoso JA, Cava F. Structural basis for the broad specificity of a new family of amino-acid racemases. Acta Crystallogr D Biol Crystallogr. 2014 Jan;70(Pt 1):79-90. doi:, 10.1107/S1399004713024838. Epub 2013 Dec 24. PMID:24419381 doi:http://dx.doi.org/10.1107/S1399004713024838
- ↑ Espaillat A, Carrasco-Lopez C, Bernardo-Garcia N, Pietrosemoli N, Otero LH, Alvarez L, de Pedro MA, Pazos F, Davis BM, Waldor MK, Hermoso JA, Cava F. Structural basis for the broad specificity of a new family of amino-acid racemases. Acta Crystallogr D Biol Crystallogr. 2014 Jan;70(Pt 1):79-90. doi:, 10.1107/S1399004713024838. Epub 2013 Dec 24. PMID:24419381 doi:http://dx.doi.org/10.1107/S1399004713024838
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