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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: รข-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