View source for 4bhy


==Structure of alanine racemase from Aeromonas hydrophila==
<StructureSection load='4bhy' size='340' side='right'caption='[[4bhy]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.25&#8491;</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'>[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>
== Function ==
[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;">
== 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<ref>PMID:24419381</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bhy" style="background-color:#fffaf0;"></div>

==See Also==
*[[Alanine racemase 3D structures|Alanine racemase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aeromonas hydrophila subsp. hydrophila]]
[[Category: Large Structures]]
[[Category: Bernardo-Garcia N]]
[[Category: Carrasco-Lopez C]]
[[Category: Hermoso JA]]
[[Category: Otero LH]]