2OLV

Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex

2OLV の概要

• エントリーDOI: 10.2210/pdb2olv/pdb
• 関連するPDBエントリー: 2OLU
• 分子名称: Penicillin-binding protein 2, MOENOMYCIN (2 entities in total)
• 機能のキーワード: transpeptidase fold, glycosyltransferase family 51, lysozyme fold, transferase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 152441.42

構造登録者

Lovering, A.L.,De Castro, L.,Lim, D.,Strynadka, N.C.J. (登録日: 2007-01-19, 公開日: 2007-03-13, 最終更新日: 2024-11-13)

主引用文献

Lovering, A.L.,de Castro, L.H.,Lim, D.,Strynadka, N.C.
Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis.
Science, 315:1402-1405, 2007

PubMed Abstract: Peptidoglycan glycosyltransferases (GTs) catalyze the polymerization step of cell-wall biosynthesis, are membrane-bound, and are highly conserved across all bacteria. Long considered the "holy grail" of antibiotic research, they represent an essential and easily accessible drug target for antibiotic-resistant bacteria, including methicillin-resistant Staphylococcus aureus. We have determined the 2.8 angstrom structure of a bifunctional cell-wall cross-linking enzyme, including its transpeptidase and GT domains, both unliganded and complexed with the substrate analog moenomycin. The peptidoglycan GTs adopt a fold distinct from those of other GT classes. The structures give insight into critical features of the catalytic mechanism and key interactions required for enzyme inhibition.

PubMed: 17347437
DOI: 10.1126/science.1136611

実験手法

X-RAY DIFFRACTION (2.8 Å)