Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components

Keitaro Yamashita, Yuka Kawai, Yoshikazu Tanaka, Nagisa Hirano, Jun Kaneko, Noriko Tomita, Makoto Ohta, Yoshiyuki Kamio, Min Yao, Isao Tanaka

研究成果: Article査読

112 被引用数 (Scopus)

抄録

Staphylococcal γ-hemolysin is a bicomponent pore-forming toxin composed of LukF and Hlg2. These proteins are expressed as water-soluble monomers and then assemble into the oligomeric pore form on the target cell. Here, we report the crystal structure of the octameric pore form of γ-hemolysin at 2.5 Å resolution, which is the first high-resolution structure of a β-barrel transmembrane protein composed of two proteins reported to date. The octameric assembly consists of four molecules of LukF and Hlg2 located alternately in a circular pattern, which explains the biochemical data accumulated over the past two decades. The structure, in combination with the monomeric forms, demonstrates the elaborate molecular machinery involved in pore formation by two different molecules, in which interprotomer electrostatic interactions using loops connecting β2 and β3 (loop A: Asp43-Lys48 of LukF and Lys37-Lys43 of Hlg2) play pivotal roles as the structural determinants for assembly through unwinding of the N-terminal β-strands (aminolatch) of the adjacent protomer, releasing the transmembrane stem domain folded into a β-sheet in the monomer (prestem), and interaction with the adjacent protomer.

本文言語English
ページ(範囲)17314-17319
ページ数6
ジャーナルProceedings of the National Academy of Sciences of the United States of America
108
42
DOI
出版ステータスPublished - 2011 10 18

ASJC Scopus subject areas

  • 一般

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