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5kmt

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<StructureSection load='5kmt' size='340' side='right'caption='[[5kmt]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='5kmt' size='340' side='right'caption='[[5kmt]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5kmt]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KMT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5KMT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5kmt]] is a 2 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=5KMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KMT FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kmu|5kmu]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5kmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kmt OCA], [https://pdbe.org/5kmt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kmt RCSB], [https://www.ebi.ac.uk/pdbsum/5kmt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kmt ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5kmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kmt OCA], [http://pdbe.org/5kmt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kmt RCSB], [http://www.ebi.ac.uk/pdbsum/5kmt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kmt ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9L5C8_ECOLX Q9L5C8_ECOLX]
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The CTX-M family of beta lactamases mediate broad-spectrum antibiotic resistance and are present in the majority of drug-resistant Gram-negative bacterial infections worldwide. Allosteric mutations that increase catalytic rates of these drug resistance enzymes have been identified in clinical isolates but are challenging to predict prospectively. We have used molecular dynamics simulations to predict allosteric mutants increasing CTX-M9 drug resistance, experimentally testing top mutants using multiple antibiotics. Purified enzymes show an increase in catalytic rate and efficiency, while mutant crystal structures show no detectable changes from wild-type CTX-M9. We hypothesize that increased drug resistance results from changes in the conformational ensemble of an acyl intermediate in hydrolysis. Machine-learning analyses on the three top mutants identify changes to the binding-pocket conformational ensemble by which these allosteric mutations transmit their effect. These findings show how molecular simulation can predict how allosteric mutations alter active-site conformational equilibria to increase catalytic rates and thus resistance against common clinically used antibiotics.
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Predicting allosteric mutants that increase activity of a major antibiotic resistance enzyme.,Latallo MJ, Cortina GA, Faham S, Nakamoto RK, Kasson PM Chem Sci. 2017 Sep 1;8(9):6484-6492. doi: 10.1039/c7sc02676e. Epub 2017 Jul 19. PMID:28989673<ref>PMID:28989673</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5kmt" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Beta-lactamase]]
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Faham, S]]
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[[Category: Faham S]]
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[[Category: Kasson, P M]]
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[[Category: Kasson PM]]
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[[Category: Latallo, M J]]
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[[Category: Latallo MJ]]
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[[Category: Beta lactamase]]
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[[Category: Esbl]]
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[[Category: Hydrolase]]
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Current revision

CTX-M9 mutant L48A

PDB ID 5kmt

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