6I1I

Crystal structure of TP domain from Escherichia coli penicillin-binding protein 3 in complex with penicillin

6I1I の概要

• エントリーDOI: 10.2210/pdb6i1i/pdb
• 関連するPDBエントリー: 6HZH 6HZI 6HZJ 6HZO 6HZQ 6HZR
• 分子名称: Peptidoglycan D,D-transpeptidase FtsI,Peptidoglycan D,D-transpeptidase FtsI, Piperacillin (Open Form) (3 entities in total)
• 機能のキーワード: penicillin-binding protein, peptidoglycan, transpeptidase, peptide binding protein
• 由来する生物種: Escherichia coli O157:H7; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37648.99

構造登録者

Bellini, D.,Koekemoer, L.,Newman, H.,Dowson, C.G. (登録日: 2018-10-28, 公開日: 2019-11-20, 最終更新日: 2024-01-24)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.75 Å)