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7xhx
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of metallo-beta-lactamase IMP-6== | |
| + | <StructureSection load='7xhx' size='340' side='right'caption='[[7xhx]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7xhx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6lvj 6lvj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XHX FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7xhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xhx OCA], [https://pdbe.org/7xhx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xhx RCSB], [https://www.ebi.ac.uk/pdbsum/7xhx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xhx ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/K4PWX3_ECOLX K4PWX3_ECOLX] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | IMP-type metallo-beta-lactamases confer resistance to carbapenems and a broad spectrum of beta-lactam antibiotics. IMP-6 and IMP-1 differ by only a point mutation: Ser262 in IMP-1 and Gly262 in IMP-6. The kcat/Km values of IMP-1 for imipenem and meropenem are nearly identical; however, for IMP-6, the kcat/Km for meropenem is 7-fold that for imipenem. In clinical practice, this may result in an ineffective therapeutic regimen and, consequently, in treatment failure. Here, we report the crystal structures of IMP-6 and IMP-1 with the same space group and similar cell constants at resolutions of 1.70 and 1.94 A, respectively. The overall structures of IMP-6 and IMP-1 are similar. However, the loop region (residues 60-66), which participates in substrate binding, is more flexible in IMP-6 than in IMP-1. This difference in flexibility determines the substrate specificity of IMP-type metallo-beta-lactamases for imipenem and meropenem. The amino acid at position 262 alters the mobility of His263; this affects the flexibility of the loop via a hydrogen bond with Pro68, which plays the role of a hinge in IMP-type metallo-beta-lactamases. The substitution of Pro68 with a glycine elicited an increase in the Km of IMP-6 for imipenem, whereas the affinity for meropenem remained unchanged. | ||
| - | + | Structural insights into the substrate specificity of IMP-6 and IMP-1 metallo-beta-lactamases.,Yamamoto K, Tanaka H, Kurisu G, Nakano R, Yano H, Sakai H J Biochem. 2022 Dec 27;173(1):21-30. doi: 10.1093/jb/mvac080. PMID:36174533<ref>PMID:36174533</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7xhx" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: Sakai | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: Yano | + | [[Category: Escherichia coli]] |
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kurisu G]] | ||
| + | [[Category: Nakano R]] | ||
| + | [[Category: Sakai H]] | ||
| + | [[Category: Tanaka H]] | ||
| + | [[Category: Yamamoto K]] | ||
| + | [[Category: Yano H]] | ||
Revision as of 10:17, 15 February 2023
Crystal structure of metallo-beta-lactamase IMP-6
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Categories: Escherichia coli | Large Structures | Kurisu G | Nakano R | Sakai H | Tanaka H | Yamamoto K | Yano H
