4KQO

Crystal structure of penicillin-binding protein 3 from pseudomonas aeruginosa in complex with piperacillin

Summary for 4KQO

• Entry DOI: 10.2210/pdb4kqo/pdb
• Related: 4KQQ 4KQR
• Descriptor: Penicillin-binding protein 3, Piperacillin (Open Form), GLYCEROL, ... (6 entities in total)
• Functional Keywords: penicillin-binding proteins, piperacillin, cell wall biosynthesis, transpeptidase, out periplasmic membrane, biosynthetic protein-antibiotic complex, biosynthetic protein/antibiotic
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 2
• Total formula weight: 123760.60

Authors

Nettleship, J.E.,Stuart, D.I.,Owens, R.J.,Ren, J. (deposition date: 2013-05-15, release date: 2013-11-06, Last modification date: 2024-10-30)

Primary citation

van Berkel, S.S.,Nettleship, J.E.,Leung, I.K.,Brem, J.,Choi, H.,Stuart, D.I.,Claridge, T.D.,McDonough, M.A.,Owens, R.J.,Ren, J.,Schofield, C.J.
Binding of (5S)-Penicilloic Acid to Penicillin Binding Protein 3.
Acs Chem.Biol., 8:2112-2116, 2013

PubMed Abstract: β-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.

PubMed: 23899657
DOI: 10.1021/cb400200h

Experimental method

X-RAY DIFFRACTION (2.31 Å)