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==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 16:51, 27 April 2017
Apo KPC-2 beta-lactamase crystal structure at 1.15 Angstrom resolutionApo KPC-2 beta-lactamase crystal structure at 1.15 Angstrom resolution
Structural highlights
Function[BLKPC_KLEPN] Hydrolyzes carbapenems, penicillins, cephalosporins and monobactams with varying efficiency. Publication Abstract from PubMedCarbapenem-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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