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5b3r
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of metallo-beta-lactamase IMP-18 from Pseudomonas aeruginosa== | |
| + | <StructureSection load='5b3r' size='340' side='right' caption='[[5b3r]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5b3r]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B3R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B3R FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <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> | ||
| + | <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=5b3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b3r OCA], [http://pdbe.org/5b3r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b3r RCSB], [http://www.ebi.ac.uk/pdbsum/5b3r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b3r ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | IMP-type metallo-beta-lactamases (MBLs) are exogenous zinc metalloenzymes that hydrolyze a broad range of beta-lactams, including carbapenems. Here we report the crystal structure of IMP-18, an MBL cloned from Pseudomonas aeruginosa, at 2.0-A resolution. The overall structure of IMP-18 resembles that of IMP-1, with an alphabeta/betaalpha "folded sandwich" configuration, but the loop that covers the active site has a distinct conformation. The relationship between IMP-18's loop conformation and its kinetic properties was investigated by replacing the amino acid residues that can affect the loop conformation (Lys44, Thr50, and Ile69) in IMP-18 with those occupying the corresponding positions in the well-described enzyme IMP-1. The replacement of Thr50 with Pro considerably modified IMP-18's kinetic properties, specifically those pertaining to meropenem, with the kcat/Km value increased by an order of magnitude. The results indicate that this is a key residue that defines the kinetic properties of IMP-type beta-lactamases. | ||
| - | + | Structural and Mutagenic Analysis of Metallo-beta-Lactamase IMP-18.,Furuyama T, Nonomura H, Ishii Y, Hanson ND, Shimizu-Ibuka A Antimicrob Agents Chemother. 2016 Aug 22;60(9):5521-6. doi: 10.1128/AAC.00985-16., Print 2016 Sep. PMID:27381398<ref>PMID:27381398</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5b3r" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Beta-lactamase]] | ||
| + | [[Category: Ishii, Y]] | ||
| + | [[Category: Shimizu-Ibuka, A]] | ||
| + | [[Category: Antibiotic resistance]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Metallo-beta-lactamase]] | ||
Revision as of 17:34, 10 March 2017
Crystal structure of metallo-beta-lactamase IMP-18 from Pseudomonas aeruginosa
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