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Crystal structure of a core domain of stomatin from Pyrococcus horikoshii Illustrates a novel trimeric and coiled-coil fold.

Crystal structure of a core domain of stomatin from Pyrococcus horikoshii Illustrates a novel trimeric and coiled-coil fold. Research Abstract Details 

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  • Crystal structure of a core domain of stomatin from Pyrococcus horikoshii Illustrates a novel trimeric and coiled-coil fold. Abstract Text:

    hideshi yokoyamaHideshi Yokoyama,satoshi fujiiSatoshi Fujii,ikuo matsuiIkuo Matsui,hideshi yokoyamaHideshi Yokoyama,satoshi fujiiSatoshi Fujii,ikuo matsuiIkuo Matsui,

    Stomatin is a major integral membrane protein of human erythrocytes, the absence of which is associated with a form of hemolytic anemia known as hereditary stomatocytosis. However, the function of stomatin is not fully understood. An open reading frame, PH1511, from the hyperthermophilic archaeon Pyrococcus horikoshii encodes p-stomatin, a prokaryotic stomatin. Here, we report the first crystal structure of a stomatin ortholog, the core domain of the p-stomatin PH1511p (residues 56-234 of PH1511p, designated as PhSto(CD)). PhSto(CD) forms a novel homotrimeric structure. Three alpha/beta domains form a triangle of about 50 A on each side, and three alpha-helical segments of about 60 A in length extend from the apexes of the triangle. The alpha/beta domain of PhSto(CD) is partly similar in structure to the band-7 domain of mouse flotillin-2. While the alpha/beta domain is relatively rigid, the alpha-helical segment shows conformational flexibility, adapting to the neighboring environment. One alpha-helical segment forms an anti-parallel coiled coil with another alpha-helical segment from a symmetry-related molecule. The alpha-helical segment shows a heptad repeat pattern, and mainly hydrophobic residues form a coiled-coil interface. According to chemical cross-linking experiments, PhSto(CD) would be able to assemble into an oligomeric form. The coiled-coil fold observed in the crystal probably contributes to self-association.

    Crystal structure of a core domain of stomatin from Pyrococcus horikoshii Illustrates a novel trimeric and coiled-coil fold. Publishing Authors By Initials

    h yokoyamaH Yokoyama,s fujiiS Fujii,i matsuiI Matsui,h yokoyamaH Yokoyama,s fujiiS Fujii,i matsuiI Matsui,

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    Crystal structure of a core domain of stomatin from Pyrococcus horikoshii Illustrates a novel trimeric and coiled-coil fold. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of molecular biology

    VOLUME: 376

    Page Numbers: 868-78

    Journal Abbreviation: J. Mol. Biol.

    ISSN: 1089-8638

    DAY: 8

    MONTH: 01

    YEAR: 2008

    Crystal structure of a core domain of stomatin from Pyrococcus horikoshii Illustrates a novel trimeric and coiled-coil fold. Information

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    LANGUAGE: eng

    NlmUniqueID: 2985088

    Crystal structure of a core domain of stomatin from Pyrococcus horikoshii Illustrates a novel trimeric and coiled-coil fold. Keywords Mesh Terms:

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    Grant and Affiliation Information for Crystal structure of a core domain of stomatin from Pyrococcus horikoshii Illustrates a novel trimeric and coiled-coil fold.

    AFFILIATION: School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka 422-8526, Japan.

    Country: England

    England Research PublicationEngland Research Publication

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    MEDLINETA: J Mol Biol

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    ACCESSION NUMBER: 3BK6

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    Crystal structure of a core domain of stomatin from Pyrococcus horikoshii Illustrates a novel trimeric and coiled-coil fold Related Publications

     

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