4P1X

Crystal structure of staphylococcal LUK prepore

4P1X の概要

• エントリーDOI: 10.2210/pdb4p1x/pdb
• 関連するPDBエントリー: 1luk 2luk 3b07 3luk 4P1Y 4P24
• 分子名称: Gamma-hemolysin component C, Gamma-hemolysin component B, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• 機能のキーワード: pore forming toxin, toxin
• 由来する生物種: Staphylococcus aureus; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 276979.04

構造登録者

Yamashita, D.,Tanaka, Y.,Tanaka, I.,Yao, M. (登録日: 2014-02-28, 公開日: 2014-10-01, 最終更新日: 2023-12-27)

主引用文献

Yamashita, D.,Sugawara, T.,Takeshita, M.,Kaneko, J.,Kamio, Y.,Tanaka, I.,Tanaka, Y.,Yao, M.
Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins.
Nat Commun, 5:4897-4897, 2014

PubMed Abstract: Pathogenic bacteria secrete pore-forming toxins (PFTs) to attack target cells. PFTs are expressed as water-soluble monomeric proteins, which oligomerize into nonlytic prepore intermediates on the target cell membrane before forming membrane-spanning pores. Despite a wealth of biochemical data, the lack of high-resolution prepore structural information has hampered understanding of the β-barrel formation process. Here, we report crystal structures of staphylococcal γ-haemolysin and leucocidin prepores. The structures reveal a disordered bottom half of the β-barrel corresponding to the transmembrane region, and a rigid upper extramembrane half. Spectroscopic analysis of fluorescently labelled mutants confirmed that the prepore is distinct from the pore within the transmembrane region. Mutational analysis also indicates a pivotal role for the glycine residue located at the lipid-solvent interface as a 'joint' between the two halves of the β-barrel. These observations suggest a two-step transmembrane β-barrel pore formation mechanism in which the upper extramembrane and bottom transmembrane regions are formed independently.

PubMed: 25263813
DOI: 10.1038/ncomms5897

実験手法

X-RAY DIFFRACTION (2.4 Å)