7s0v: Difference between revisions
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New page: '''Unreleased structure''' The entry 7s0v is ON HOLD Authors: Kemp, M.T., Chen, Y. Description: The role of an Asp-Asp pair in the structure, function and inhibition of CTX-M Class A B... |
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The | ==The role of an Asp-Asp pair in the structure, function and inhibition of CTX-M Class A Beta-lactamase== | ||
<StructureSection load='7s0v' size='340' side='right'caption='[[7s0v]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7s0v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7S0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7S0V 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]] 1.95Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=J1X:3-(1H-pyrazol-1-yl)-N-[3-(1H-tetrazol-5-yl)phenyl]-5-(trifluoromethyl)benzamide'>J1X</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=7s0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7s0v OCA], [https://pdbe.org/7s0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7s0v RCSB], [https://www.ebi.ac.uk/pdbsum/7s0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7s0v ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9L5C7_ECOLX Q9L5C7_ECOLX] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Asp233-Asp246 pair is highly conserved in Class A beta-lactamases, which hydrolyze beta-lactam antibiotics. Here, we characterize its function using CTX-M-14 beta-lactamase. The D233N mutant displayed decreased activity that is substrate-dependent, with reductions in kcat /Km ranging from 20% for nitrocefin to 6-fold for cefotaxime. In comparison, the mutation reduced the binding of a known reversible inhibitor by 10-fold. The mutant structures showed movement of the 213-219 loop and the loss of the Thr216-Thr235 hydrogen bond, which was restored by inhibitor binding. Mutagenesis of Thr216 further highlighted its contribution to CTX-M activity. These results demonstrate the importance of the aspartate pair to CTX-M hydrolysis of substrates with bulky side chains, while suggesting increased protein flexibility as a means to evolve drug resistance. | |||
Mutation of the conserved Asp-Asp pair impairs the structure, function, and inhibition of CTX-M Class A beta-lactamase.,Kemp MT, Nichols DA, Zhang X, Defrees K, Na I, Renslo AR, Chen Y FEBS Lett. 2021 Oct 26. doi: 10.1002/1873-3468.14215. PMID:34704263<ref>PMID:34704263</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7s0v" style="background-color:#fffaf0;"></div> | ||
[[Category: Chen | |||
==See Also== | |||
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Chen Y]] | |||
[[Category: Kemp MT]] | |||
Latest revision as of 10:42, 22 May 2024
The role of an Asp-Asp pair in the structure, function and inhibition of CTX-M Class A Beta-lactamase
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