3opr

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<StructureSection load='3opr' size='340' side='right'caption='[[3opr]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='3opr' size='340' side='right'caption='[[3opr]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3opr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_pneumoniae"_(schroeter_1886)_flugge_1886 "bacillus pneumoniae" (schroeter 1886) flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OPR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3opr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OPR 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=MA4:CYCLOHEXYL-HEXYL-BETA-D-MALTOSIDE'>MA4</scene>, <scene name='pdbligand=SA2:(3R)-4-[(4-CARBOXYBUTANOYL)OXY]-N-[(1E)-3-OXOPROP-1-EN-1-YL]-3-SULFINO-D-VALINE'>SA2</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]] 1.65&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2h5s|2h5s]], [[3oph|3oph]], [[3opl|3opl]], [[3opp|3opp]]</div></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=MA4:CYCLOHEXYL-HEXYL-BETA-D-MALTOSIDE'>MA4</scene>, <scene name='pdbligand=SA2:(3R)-4-[(4-CARBOXYBUTANOYL)OXY]-N-[(1E)-3-OXOPROP-1-EN-1-YL]-3-SULFINO-D-VALINE'>SA2</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bla, shv1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=573 "Bacillus pneumoniae" (Schroeter 1886) Flugge 1886])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [https://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=3opr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3opr OCA], [https://pdbe.org/3opr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3opr RCSB], [https://www.ebi.ac.uk/pdbsum/3opr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3opr ProSAT]</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=3opr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3opr OCA], [https://pdbe.org/3opr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3opr RCSB], [https://www.ebi.ac.uk/pdbsum/3opr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3opr ProSAT]</span></td></tr>
</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/BLA1_KLEPN BLA1_KLEPN]
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Among Gram-negative bacteria, resistance to beta-lactams is mediated primarily by beta-lactamases (EC 3.2.6.5), periplasmic enzymes that inactivate beta-lactam antibiotics. Substitutions at critical amino acid positions in the class A beta-lactamase families result in enzymes that can hydrolyze extended-spectrum cephalosporins, thus demonstrating an "extended-spectrum" beta-lactamase (ESBL) phenotype. Using SHV ESBLs with substitutions in the Omega loop (R164H and R164S) as target enzymes to understand this enhanced biochemical capability and to serve as a basis for novel beta-lactamase inhibitor development, we determined the spectra of activity and crystal structures of these variants. We also studied the inactivation of the R164H and R164S mutants with tazobactam and SA2-13, a unique beta-lactamase inhibitor that undergoes a distinctive reaction chemistry in the active site. We noted that the reduced Ki values for the R164H and R164S mutants with SA2-13 are comparable to those with tazobactam (submicromolar). The apo enzyme crystal structures of the R164H and R164S SHV variants revealed an ordered Omega loop architecture that became disordered when SA2-13 was bound. Important structural alterations that result from the binding of SA2-13 explain the enhanced susceptibility of these ESBL enzymes to this inhibitor and highlight ligand-dependent Omega loop flexibility as a mechanism for accommodating and hydrolyzing beta-lactam substrates.
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Ligand-dependent disorder of the Omega loop observed in extended-spectrum SHV-type beta-lactamase.,Sampson JM, Ke W, Bethel CR, Pagadala SR, Nottingham MD, Bonomo RA, Buynak JD, van den Akker F Antimicrob Agents Chemother. 2011 May;55(5):2303-9. Epub 2011 Feb 28. PMID:21357298<ref>PMID:21357298</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 3opr" 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: Klebsiella pneumoniae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Akker, F van den]]
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[[Category: Sampson JM]]
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[[Category: Sampson, J M]]
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[[Category: Van den Akker F]]
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[[Category: Class a beta-lactamase]]
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[[Category: Hydrolase]]
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Revision as of 11:18, 21 February 2024

ESBL R164H mutant of SHV-1 beta-lactamase complexed to SA2-13

PDB ID 3opr

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