1PMD

PENICILLIN-BINDING PROTEIN 2X (PBP-2X)

1PMD の概要

• エントリーDOI: 10.2210/pdb1pmd/pdb
• 分子名称: PEPTIDOGLYCAN SYNTHESIS MULTIFUNCTIONAL ENZYME (1 entity in total)
• 機能のキーワード: peptidoglycan synthesis, resistance, cell wall, transmembrane
• 由来する生物種: Streptococcus pneumoniae
• 細胞内の位置: Cell membrane; Single-pass membrane protein: P14677
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 73919.66

構造登録者

Pares, S.,Mouz, N.,Dideberg, O. (登録日: 1996-02-05, 公開日: 1997-02-05, 最終更新日: 2024-02-14)

主引用文献

Pares, S.,Mouz, N.,Petillot, Y.,Hakenbeck, R.,Dideberg, O.
X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme.
Nat.Struct.Biol., 3:284-289, 1996

PubMed Abstract: All beta-lactam antibiotics exert their biological effects by interacting with a unique class of proteins, the penicillin-binding proteins (PBPs). These membrane proteins are involved in the biosynthesis of the murein or peptidoglycan, a mesh-like structure which completely surrounds the bacterial cell. Sequence similarities indicate that one domain of these proteins belongs to a large family of beta-lactam-recognizing proteins, which includes the active-site serine beta-lactamases. We here report the first three-dimensional crystal structure of a high molecular weight penicillin-binding protein, PBP2x of Streptococcus pneumoniae, at 3.5 A resolution. The molecule has three domains, the central domain being a transpeptidase, which is a suitable target for antibiotic development.

PubMed: 8605631
DOI: 10.1038/nsb0396-284

実験手法

X-RAY DIFFRACTION (3.5 Å)