3VMA

Crystal Structure of the Full-Length Transglycosylase PBP1b from Escherichia coli

「3FWM」から置き換えられました

3VMA の概要

• エントリーDOI: 10.2210/pdb3vma/pdb
• 関連するPDBエントリー: 3FWL
• 分子名称: Penicillin-binding protein 1B, MOENOMYCIN (3 entities in total)
• 機能のキーワード: bacterial cell wall synthesis, penicillin-binding protein, antibiotics design, pbp3, mipa, mlta, ftsn, membrane, transferase, hydrolase-antibiotic complex, hydrolase/antibiotic
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Single-pass type II membrane protein: P02919
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 87163.48

構造登録者

Huang, C.Y.,Sung, M.T.,Lai, Y.T.,Chou, L.Y.,Shih, H.W.,Cheng, W.C.,Wong, C.H.,Ma, C. (登録日: 2011-12-09, 公開日: 2012-03-14, 最終更新日: 2023-11-08)

主引用文献

Sung, M.T.,Lai, Y.T.,Huang, C.Y.,Chou, L.Y.,Shih, H.W.,Cheng, W.C.,Wong, C.H.,Ma, C.
Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli.
Proc.Natl.Acad.Sci.USA, 106:8824-8829, 2009

PubMed Abstract: Drug-resistant bacteria have caused serious medical problems in recent years, and the need for new antibacterial agents is undisputed. Transglycosylase, a multidomain membrane protein essential for cell wall synthesis, is an excellent target for the development of new antibiotics. Here, we determined the X-ray crystal structure of the bifunctional transglycosylase penicillin-binding protein 1b (PBP1b) from Escherichia coli in complex with its inhibitor moenomycin to 2.16-A resolution. In addition to the transglycosylase and transpeptidase domains, our structure provides a complete visualization of this important antibacterial target, and reveals a domain for protein-protein interaction and a transmembrane helix domain essential for substrate binding, enzymatic activity, and membrane orientation.

PubMed: 19458048
DOI: 10.1073/pnas.0904030106

実験手法

X-RAY DIFFRACTION (2.161 Å)