4WVG

Crystal structure of the Type-I signal peptidase from Staphylococcus aureus (SpsB).

4WVG の概要

• エントリーDOI: 10.2210/pdb4wvg/pdb
• 関連するPDBエントリー: 4WVH 4WVI 4WVJ
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Maltose-binding periplasmic protein,Signal peptidase IB, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• 機能のキーワード: spsb type-i signal peptidase, cell secretion, mbp fusion protein, hydrolase
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 60644.25

構造登録者

Young, P.G.,Ting, Y.T.,Baker, E.N. (登録日: 2014-11-05, 公開日: 2015-09-23, 最終更新日: 2023-09-27)

主引用文献

Ting, Y.T.,Harris, P.W.,Batot, G.,Brimble, M.A.,Baker, E.N.,Young, P.G.
Peptide binding to a bacterial signal peptidase visualized by peptide tethering and carrier-driven crystallization.
IUCrJ, 3:10-19, 2016

PubMed Abstract: Bacterial type I signal peptidases (SPases) are membrane-anchored serine proteases that process the signal peptides of proteins exported via the Sec and Tat secretion systems. Despite their crucial importance for bacterial virulence and their attractiveness as drug targets, only one such enzyme, LepB from Escherichia coli, has been structurally characterized, and the transient nature of peptide binding has stymied attempts to directly visualize SPase-substrate complexes. Here, the crystal structure of SpsB, the type I signal peptidase from the Gram-positive pathogen Staphylococcus aureus, is reported, and a peptide-tethering strategy that exploits the use of carrier-driven crystallization is described. This enabled the determination of the crystal structures of three SpsB-peptide complexes, both with cleavable substrates and with an inhibitory peptide. SpsB-peptide interactions in these complexes are almost exclusively limited to the canonical signal-peptide motif Ala-X-Ala, for which clear specificity pockets are found. Minimal contacts are made outside this core, with the variable side chains of the peptides accommodated in shallow grooves or exposed faces. These results illustrate how high fidelity is retained despite broad sequence diversity, in a process that is vital for cell survival.

PubMed: 26870377
DOI: 10.1107/S2052252515019971

実験手法

X-RAY DIFFRACTION (2.05 Å)