Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components. Supporting Information
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چکیده
Title Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components Author(s) Yamashita, Keitaro; Kawai, Yuka; Tanaka, Yoshikazu; Hirano, Nagisa; Kaneko, Jun; Tomita, Noriko; Ohta, Makoto; Kamio, Yoshiyuki; Yao, Min; Tanaka, Isao Citation Proceedings of the National Academy of Sciences of the United States of America, 108(42): 1731417319 Issue Date 2011-10-18 Doc URL http://hdl.handle.net/2115/49037 Type article (author version) Additional Information There are other files related to this item in HUSCAP. Check the above URL. File Information Supporting_Information.pdf (Supporting Information)
منابع مشابه
Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components.
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 co...
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