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

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

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    12 Citations (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.

    Original languageEnglish
    Pages (from-to)1045-1053
    Number of pages9
    JournalActa Crystallographica Section D: Biological Crystallography
    Issue number12
    Publication statusPublished - 2011 Dec


    • Β-propellers
    • DNA
    • YncE

    ASJC Scopus subject areas

    • Structural Biology


    Dive into the research topics of 'Structural basis for the DNA-binding activity of the bacterial Β-propeller protein YncE'. Together they form a unique fingerprint.

    Cite this