5ul8
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Apo KPC-2 beta-lactamase crystal structure at 1.15 Angstrom resolution== | |
| + | <StructureSection load='5ul8' size='340' side='right' caption='[[5ul8]], [[Resolution|resolution]] 1.15Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ul8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UL8 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uj3|5uj3]], [[5uj4|5uj4]]</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=5ul8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ul8 OCA], [http://pdbe.org/5ul8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ul8 RCSB], [http://www.ebi.ac.uk/pdbsum/5ul8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ul8 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/BLKPC_KLEPN BLKPC_KLEPN]] Hydrolyzes carbapenems, penicillins, cephalosporins and monobactams with varying efficiency. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Carbapenem-resistant Enterobacteriaceae are resistant to most beta-lactam antibiotics due to the production of the Klebsiella pneumoniae carbapenemase (KPC-2) class A beta-lactamase. Here, we present the first product complex crystal structures of KPC-2 with beta-lactam antibiotics containing hydrolyzed cefotaxime and faropenem. They provide experimental insights into substrate recognition by KPC-2 and its unique cephalosporinase/carbapenemase activity. These structures also represent the first product complexes for a wild-type serine beta-lactamase, elucidating the product release mechanism of these enzymes in general. | ||
| - | + | Molecular Basis of Substrate Recognition and Product Release by the Klebsiella pneumoniae Carbapenemase (KPC-2).,Pemberton OA, Zhang X, Chen Y J Med Chem. 2017 Apr 17. doi: 10.1021/acs.jmedchem.7b00158. PMID:28388065<ref>PMID:28388065</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 5ul8" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Beta-lactamase]] | ||
[[Category: Chen, Y]] | [[Category: Chen, Y]] | ||
| + | [[Category: Pemberton, O A]] | ||
| + | [[Category: Carbapenemase]] | ||
| + | [[Category: High-resolution]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Klebsiella]] | ||
Revision as of 13:51, 27 April 2017
Apo KPC-2 beta-lactamase crystal structure at 1.15 Angstrom resolution
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