2FFF

Open Form of a Class A Transpeptidase Domain

2FFF の概要

• エントリーDOI: 10.2210/pdb2fff/pdb
• 分子名称: penicillin-binding protein 1B, NICKEL (II) ION, ... (4 entities in total)
• 機能のキーワード: transpeptidase fold, membrane protein, transferase
• 由来する生物種: Streptococcus pneumoniae; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51500.75

構造登録者

Lovering, A.L.,Strynadka, N.C.J. (登録日: 2005-12-19, 公開日: 2006-06-20, 最終更新日: 2023-08-30)

主引用文献

Lovering, A.L.,De Castro, L.,Lim, D.,Strynadka, N.C.
Structural analysis of an "open" form of PBP1B from Streptococcus pneumoniae.
Protein Sci., 15:1701-1709, 2006

PubMed Abstract: The class A PBP1b from Streptococcus pneumoniae is responsible for glycosyltransferase and transpeptidase (TP) reactions, forming the peptidoglycan of the bacterial cell wall. The enzyme has been produced in a stable, soluble form and undergoes time-dependent proteolysis to leave an intact TP domain. Crystals of this TP domain were obtained, diffracting to 2.2 A resolution, and the structure was solved by using molecular replacement. Analysis of the structure revealed an "open" active site, with important conformational differences to the previously determined "closed" apoenzyme. The active-site nucleophile, Ser460, is in an orientation that allows for acylation by beta-lactams. Consistent with the productive conformation of the conserved active-site catalytic residues, adjacent loops show only minor deviation from those of known acyl-enzyme structures. These findings are discussed in the context of enzyme functionality and the possible conformational sampling of PBP1b between active and inactive states.

PubMed: 16751607
DOI: 10.1110/ps.062112106

実験手法

X-RAY DIFFRACTION (2.23 Å)