Structural basis for the DNA-binding activity of the bacterial Β-propeller protein YncE

Wataru Kagawa, Tomohiko Sagawa, Hironori Niki, Hitoshi Kurumizaka*


    研究成果: Article査読

    12 被引用数 (Scopus)


    Β-Propellers are widely utilized in nature as recognition modules. The well conserved Β-propeller fold exhibits a high degree of functional diversity, which is probably accomplished through variations in the surface properties of the proteins. Little is known about the interactions between Β-propeller proteins and nucleic acids. In the present study, it has been found that the bacterial Β-propeller protein YncE binds to DNA. Crystal structures of YncE in the free form and complexed with DNA revealed that the surface region of YncE corresponding to the canonical substrate-binding site forms essential contacts with DNA. A single DNA base within a single-stranded DNA region is trapped in the hydrophobic pocket located within the central channel of the Β-propeller protein. These data provide physical evidence for the DNA-binding ability of the previously uncharacterized YncE and also suggest that the canonical substrate-binding site may be commonly adapted to facilitate nucleic acid binding in a subset of Β-propeller proteins.

    ジャーナルActa Crystallographica Section D: Biological Crystallography
    出版ステータスPublished - 2011 12月

    ASJC Scopus subject areas

    • 構造生物学


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