View source for 6q70


==Crystal structure of the alanine racemase Bsu17640 from Bacillus subtilis in the presence of HEPES==
<StructureSection load='6q70' size='340' side='right'caption='[[6q70]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6q70]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Q70 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]] 2.05&#8491;</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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=6q70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q70 OCA], [https://pdbe.org/6q70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6q70 RCSB], [https://www.ebi.ac.uk/pdbsum/6q70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6q70 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ALR2_BACSU ALR2_BACSU] Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pyridoxal 5'-phosphate (PLP) is a versatile cofactor involved in a large variety of enzymatic processes. Most of PLP-catalysed reactions, such as those of alanine racemases (AlaRs), present a common resting state in which the PLP is covalently bound to an active-site lysine to form an internal aldimine. The crystal structure of BsAlaR grown in the presence of Tris lacks this covalent linkage and the PLP cofactor appears deformylated. However, loss of activity in a Tris buffer only occurred after the solution was frozen prior to carrying out the enzymatic assay. This evidence strongly suggests that Tris can access the active site at subzero temperatures and behave as an alternate racemase substrate leading to mechanism-based enzyme inactivation, a hypothesis that is supported by additional X-ray structures and theoretical results from QM/MM calculations. Taken together, our findings highlight a possibly underappreciated role for a common buffer component widely used in biochemical and biophysical experiments.

Cold-induced aldimine bond cleavage by Tris in Bacillus subtilis alanine racemase.,Bernardo-Garcia N, Sanchez-Murcia PA, Espaillat A, Martinez-Caballero S, Cava F, Hermoso JA, Gago F Org Biomol Chem. 2019 Apr 12. doi: 10.1039/c9ob00223e. PMID:30977502<ref>PMID:30977502</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6q70" style="background-color:#fffaf0;"></div>

==See Also==
*[[Alanine racemase 3D structures|Alanine racemase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Bernardo-Garcia N]]
[[Category: Gago F]]
[[Category: Hermoso JA]]