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| | ==Structure of alanine racemase from Aeromonas hydrophila== | | ==Structure of alanine racemase from Aeromonas hydrophila== |
| - | <StructureSection load='4bhy' size='340' side='right' caption='[[4bhy]], [[Resolution|resolution]] 3.25Å' scene=''> | + | <StructureSection load='4bhy' size='340' side='right'caption='[[4bhy]], [[Resolution|resolution]] 3.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4bhy]] is a 4 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=4BHY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BHY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4bhy]] is a 4 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=4BHY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BHY FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</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]] 3.25Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></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=4bhy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bhy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bhy RCSB], [http://www.ebi.ac.uk/pdbsum/4bhy PDBsum]</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=4bhy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bhy OCA], [https://pdbe.org/4bhy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bhy RCSB], [https://www.ebi.ac.uk/pdbsum/4bhy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bhy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0KH11_AERHH A0KH11_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/ALR_AERHH ALR_AERHH] Catalyzes the interconversion of L-alanine and D-alanine. Likely plays an important role in supplying D-alanine, which is an indispensable constituent in the biosynthesis of bacterial cell-wall peptidoglycan.<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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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4bhy" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Alanine racemase|Alanine racemase]] | + | *[[Alanine racemase 3D structures|Alanine racemase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Aeromonas hydrophila subsp. hydrophila]] | | [[Category: Aeromonas hydrophila subsp. hydrophila]] |
| - | [[Category: Alanine racemase]] | + | [[Category: Large Structures]] |
| - | [[Category: Bernardo-Garcia, N]] | + | [[Category: Bernardo-Garcia N]] |
| - | [[Category: Carrasco-Lopez, C]] | + | [[Category: Carrasco-Lopez C]] |
| - | [[Category: Hermoso, J A]] | + | [[Category: Hermoso JA]] |
| - | [[Category: Otero, L H]] | + | [[Category: Otero LH]] |
| - | [[Category: D-amino acid]]
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| - | [[Category: Isomerase]]
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| Structural highlights
Function
ALR_AERHH Catalyzes the interconversion of L-alanine and D-alanine. Likely plays an important role in supplying D-alanine, which is an indispensable constituent in the biosynthesis of bacterial cell-wall peptidoglycan.[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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