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

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Title: Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components
Authors: Yamashita, Keitaro Browse this author
Kawai, Yuka Browse this author
Tanaka, Yoshikazu Browse this author →KAKEN DB
Hirano, Nagisa Browse this author
Kaneko, Jun Browse this author
Tomita, Noriko Browse this author
Ohta, Makoto Browse this author
Kamio, Yoshiyuki Browse this author
Yao, Min Browse this author →KAKEN DB
Tanaka, Isao Browse this author →KAKEN DB
Issue Date: 18-Oct-2011
Publisher: National Academy of Sciences
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 108
Issue: 42
Start Page: 17314
End Page: 17319
Publisher DOI: 10.1073/pnas.1110402108
Abstract: Staphylococcal γ-hemolysin is a bi-component 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 2.5Å 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 inter-protomer 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 (amino-latch) of the adjacent protomer, releasing the transmembrane stem domain folded into a β-sheet in the monomer (pre-stem), and interaction with the adjacent protomer.
Type: article (author version)
URI: http://hdl.handle.net/2115/49037
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 田中 勲

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