2XD1

ACTIVE SITE RESTRUCTURING REGULATES LIGAND RECOGNITION IN CLASS A PENICILLIN-BINDING PROTEINS

「2UWY」から置き換えられました 「2BG4」から置き換えられました

2XD1 の概要

• エントリーDOI: 10.2210/pdb2xd1/pdb
• 関連するPDBエントリー: 2UWX 2XD5
• 分子名称: PENICILLIN-BINDING PROTEIN 1B, CEFOTAXIME, C3' cleaved, open, bound form, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: transferase, peptidoglycan synthesis, acyltransferase, glycosyltransferase, cell wall, peptidoglycan
• 由来する生物種: STREPTOCOCCUS PNEUMONIAE
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 109236.77

構造登録者

Macheboeuf, P.,Di Guilmi, A.M.,Job, V.,Vernet, T.,Dideberg, O.,Dessen, A. (登録日: 2010-04-28, 公開日: 2010-05-26, 最終更新日: 2024-11-06)

主引用文献

Macheboeuf, P.,Di Guilmi, A.M.,Job, V.,Vernet, T.,Dideberg, O.,Dessen, A.
Active Site Restructuring Regulates Ligand Recognition in Class a Penicillin-Binding Proteins.
Proc.Natl.Acad.Sci.USA, 102:577-, 2005

PubMed Abstract: Bacterial cell division is a complex, multimolecular process that requires biosynthesis of new peptidoglycan by penicillin-binding proteins (PBPs) during cell wall elongation and septum formation steps. Streptococcus pneumoniae has three bifunctional (class A) PBPs that catalyze both polymerization of glycan chains (glycosyltransfer) and cross-linking of pentapeptidic bridges (transpeptidation) during the peptidoglycan biosynthetic process. In addition to playing important roles in cell division, PBPs are also the targets for beta-lactam antibiotics and thus play key roles in drug-resistance mechanisms. The crystal structure of a soluble form of pneumococcal PBP1b (PBP1b*) has been solved to 1.9 A, thus providing previously undescribed structural information regarding a class A PBP from any organism. PBP1b* is a three-domain molecule harboring a short peptide from the glycosyltransferase domain bound to an interdomain linker region, the transpeptidase domain, and a C-terminal region. The structure of PBP1b* complexed with beta-lactam antibiotics reveals that ligand recognition requires a conformational modification involving conserved elements within the cleft. The open and closed structures of PBP1b* suggest how class A PBPs may become activated as novel peptidoglycan synthesis becomes necessary during the cell division process. In addition, this structure provides an initial framework for the understanding of the role of class A PBPs in the development of antibiotic resistance.

PubMed: 15637155
DOI: 10.1073/PNAS.0407186102

実験手法

X-RAY DIFFRACTION (3 Å)