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From Proteopedia
CRYSTAL STRUCTURE OF PENICILLIN-BINDING PROTEIN 3 FROM PSEUDOMONAS AERUGINOSA IN COMPLEX WITH (5S)-Penicilloic Acid
Structural highlights
FunctionFTSI_PSEAE Catalyzes cross-linking of the peptidoglycan cell wall at the division septum (By similarity). Binds penicillin (PubMed:20580675).[HAMAP-Rule:MF_02080][1] Publication Abstract from PubMedbeta-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. Formation of the complex was confirmed by solution studies, including NMR. Together, these results will be useful in the design of new PBP inhibitors and raise the possibility that noncovalent PBP inhibition by penicilloic acids may be of clinical relevance. Binding of (5S)-Penicilloic Acid to Penicillin Binding Protein 3.,van Berkel SS, Nettleship JE, Leung IK, Brem J, Choi H, Stuart DI, Claridge TD, McDonough MA, Owens RJ, Ren J, Schofield CJ ACS Chem Biol. 2013 Oct 18;8(10):2112-6. doi: 10.1021/cb400200h. Epub 2013 Aug, 15. PMID:23899657[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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