7KCW

Crystal structure of S. aureus penicillin-binding protein 4 (PBP4) mutant (R200L) in complex with nafcillin

Summary for 7KCW

Entry DOI	10.2210/pdb7kcw/pdb
Descriptor	Penicillin-binding protein 4, (2R,4S)-2-[(1R)-1-{[(2-ethoxynaphthalen-1-yl)carbonyl]amino}-2-oxoethyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid, GLYCEROL, ... (5 entities in total)
Functional Keywords	acyl-enzyme intermediate, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological source	Staphylococcus aureus (strain COL)
Total number of polymer chains	1
Total formula weight	41720.40
Authors	Alexander, J.A.,Strynadka, N.C. (deposition date: 2020-10-07, release date: 2021-06-30, Last modification date: 2023-10-18)
Primary citation	Satishkumar, N.,Alexander, J.A.N.,Poon, R.,Buggeln, E.,Argudin, M.A.,Strynadka, N.C.J.,Chatterjee, S.S. PBP4-mediated beta-lactam resistance among clinical strains of Staphylococcus aureus. J.Antimicrob.Chemother., 76:2268-2272, 2021 Cited by PubMed Abstract: PBP4, a low-molecular-weight PBP in Staphylococcus aureus, is not considered to be a classical mediator of β-lactam resistance. Previous studies carried out by our group with laboratory strains of S. aureus demonstrated the ability of PBP4 to produce β-lactam resistance through mutations associated with the pbp4 promoter and/or gene. Recent studies of β-lactam-resistant clinical isolates of S. aureus have reported similar mutations associated with pbp4. PubMed: 34151961 DOI: 10.1093/jac/dkab201 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.73 Å)

Structure validation