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6u58

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Current revision (14:56, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6u58' size='340' side='right'caption='[[6u58]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='6u58' size='340' side='right'caption='[[6u58]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6u58]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U58 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6U58 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6u58]] 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=6U58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6U58 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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">Hybrid , Neutron Diffraction , X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6u58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u58 OCA], [http://pdbe.org/6u58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6u58 RCSB], [http://www.ebi.ac.uk/pdbsum/6u58 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6u58 ProSAT]</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=6u58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u58 OCA], [https://pdbe.org/6u58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6u58 RCSB], [https://www.ebi.ac.uk/pdbsum/6u58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6u58 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/BLT1_ECOLX BLT1_ECOLX] Has strong cefotaxime-hydrolyzing activity.
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The amino-acid sequence of the Toho-1 beta-lactamase contains several conserved residues in the active site, including Ser70, Lys73, Ser130 and Glu166, some of which coordinate a catalytic water molecule. This catalytic water molecule is essential in the acylation and deacylation parts of the reaction mechanism through which Toho-1 inactivates specific antibiotics and provides resistance to its expressing bacterial strains. To investigate the function of Glu166 in the acylation part of the catalytic mechanism, neutron and X-ray crystallographic studies were performed on a Glu166Gln mutant. The structure of this class A beta-lactamase mutant provides several insights into its previously reported reduced drug-binding kinetic rates. A joint refinement of both X-ray and neutron diffraction data was used to study the effects of the Glu166Gln mutation on the active site of Toho-1. This structure reveals that while the Glu166Gln mutation has a somewhat limited impact on the positions of the conserved amino acids within the active site, it displaces the catalytic water molecule from the active site. These subtle changes offer a structural explanation for the previously observed decreases in the binding of non-beta-lactam inhibitors such as the recently developed diazobicyclooctane inhibitor avibactam.
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Probing the role of the conserved residue Glu166 in a class A beta-lactamase using neutron and X-ray protein crystallography.,Langan PS, Sullivan B, Weiss KL, Coates L Acta Crystallogr D Struct Biol. 2020 Feb 1;76(Pt 2):118-123. doi:, 10.1107/S2059798319016334. Epub 2020 Jan 24. PMID:32038042<ref>PMID:32038042</ref>
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==See Also==
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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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 6u58" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__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: Langan, P S]]
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[[Category: Langan PS]]
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[[Category: Sullivan, B]]
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[[Category: Sullivan B]]
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[[Category: Weiss, K L]]
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[[Category: Weiss KL]]
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[[Category: Hydrolase]]
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Current revision

Toho1 Beta Lactamase Glu166Gln Mutant

PDB ID 6u58

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