Binding of (5S)-Penicilloic Acid to Penicillin Binding Protein 3

DOI: 10.1021/cb400200h
PMID: 23899657

Authors: Sander S. Van Berkel (University of Oxford) , Joanne Nettleship (University of Oxford) , Ivanhoe K. H. Leung (University of Oxford) , Jurgen Brem (University of Oxford) , Hwanho Choi (University of Oxford) , David I. Stuart (Diamond Light Source) , Timothy D. W. Claridge (University of Oxford) , Michael A. Mcdonough (Department of Chemistry, University of Oxford) , Raymond J. Owens (University of Oxford) , Jingshan Ren (University of Oxford) , Christopher J. Schofield (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acs Chemical Biology , VOL 8 (10)

State: Published (Approved)
Published: August 2013
Diamond Proposal Number(s): 8423

Abstract: â-Lactam antibiotics react with penicillin binding proteins (PBPs) to form relatively stable acyl-enzyme complexes. We describe structures derived from the reaction of piperacillin with PBP3 Pseudomonas aeruginosa) including not only the anticipated acyl-enzyme complex but also an unprecedented complex with (5S)-penicilloic acid, which was formed by C-5 epimerization of the nascent (5R)-penicilloic acid product.

Subject Areas: Biology and Bio-materials, Chemistry, Medicine


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I24-Microfocus Macromolecular Crystallography

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