5UJ4

Crystal structure of the KPC-2 beta-lactamase complexed with hydrolyzed faropenem

Summary for 5UJ4

• Entry DOI: 10.2210/pdb5uj4/pdb
• Related: 5UJ3 5UL8
• Descriptor: Carbapenem-hydrolyzing beta-lactamase KPC, (2R)-2-[(1S,2R)-1-carboxy-2-hydroxypropyl]-5-[(2R)-oxolan-2-yl]-2,3-dihydro-1,3-thiazole-4-carboxylic acid, GLYCEROL, ... (4 entities in total)
• Functional Keywords: carbapenemase, faropenem, beta-lactamase, complex, hydrolase-antibiotic complex, hydrolase/antibiotic
• Biological source: Klebsiella pneumoniae
• Total number of polymer chains: 1
• Total formula weight: 31202.06

Authors

Pemberton, O.A.,Chen, Y. (deposition date: 2017-01-16, release date: 2017-04-26, Last modification date: 2024-10-09)

Primary citation

Pemberton, O.A.,Zhang, X.,Chen, Y.
Molecular Basis of Substrate Recognition and Product Release by the Klebsiella pneumoniae Carbapenemase (KPC-2).
J. Med. Chem., 60:3525-3530, 2017

PubMed Abstract: Carbapenem-resistant Enterobacteriaceae are resistant to most β-lactam antibiotics due to the production of the Klebsiella pneumoniae carbapenemase (KPC-2) class A β-lactamase. Here, we present the first product complex crystal structures of KPC-2 with β-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 β-lactamase, elucidating the product release mechanism of these enzymes in general.

PubMed: 28388065
DOI: 10.1021/acs.jmedchem.7b00158

Experimental method

X-RAY DIFFRACTION (1.4 Å)