6HZQ

Apo structure of TP domain from Escherichia coli Penicillin-Binding Protein 3

Summary for 6HZQ

• Entry DOI: 10.2210/pdb6hzq/pdb
• Related: 4BJP 6HZH 6HZI 6HZJ 6HZO
• Descriptor: Peptidoglycan D,D-transpeptidase FtsI (2 entities in total)
• Functional Keywords: penicillin-binding protein, peptidoglycan, transpeptidase, peptide binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 37129.42

Authors

Bellini, D.,Koekemoer, L.,Newman, H.,Dowson, C.G. (deposition date: 2018-10-23, release date: 2019-11-20, Last modification date: 2024-01-24)

Primary citation

Bellini, D.,Koekemoer, L.,Newman, H.,Dowson, C.G.
Novel and Improved Crystal Structures of H. influenzae, E. coli and P. aeruginosa Penicillin-Binding Protein 3 (PBP3) and N. gonorrhoeae PBP2: Toward a Better Understanding of beta-Lactam Target-Mediated Resistance.
J.Mol.Biol., 431:3501-3519, 2019

PubMed Abstract: Even with the emergence of antibiotic resistance, penicillin and the wider family of β-lactams have remained the single most important family of antibiotics. The periplasmic/extra-cytoplasmic targets of penicillin are a family of enzymes with a highly conserved catalytic activity involved in the final stage of bacterial cell wall (peptidoglycan) biosynthesis. Named after their ability to bind penicillin, rather than their catalytic activity, these key targets are called penicillin-binding proteins (PBPs). Resistance is predominantly mediated by reducing the target drug concentration via β-lactamases; however, naturally transformable bacteria have also acquired target-mediated resistance by inter-species recombination. Here we focus on structural based interpretations of amino acid alterations associated with the emergence of resistance within clinical isolates and include new PBP3 structures along with new, and improved, PBP-β-lactam co-structures.

PubMed: 31301409
DOI: 10.1016/j.jmb.2019.07.010

Experimental method

X-RAY DIFFRACTION (1.95 Å)