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5b3r

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<StructureSection load='5b3r' size='340' side='right'caption='[[5b3r]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='5b3r' size='340' side='right'caption='[[5b3r]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5b3r]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. 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>
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<table><tr><td colspan='2'>[[5b3r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5B3R 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=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IMP-18, blaIMP-18, blaimp-18, imp-18 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5b3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b3r OCA], [https://pdbe.org/5b3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b3r RCSB], [https://www.ebi.ac.uk/pdbsum/5b3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b3r 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://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>
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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/Q5U807_PSEAI Q5U807_PSEAI]
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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.
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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>
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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 5b3r" 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]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ishii, Y]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Shimizu-Ibuka, A]]
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[[Category: Ishii Y]]
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[[Category: Antibiotic resistance]]
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[[Category: Shimizu-Ibuka A]]
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[[Category: Hydrolase]]
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[[Category: Metallo-beta-lactamase]]
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Current revision

Crystal structure of metallo-beta-lactamase IMP-18 from Pseudomonas aeruginosa

PDB ID 5b3r

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