Crystal structure and mechanistic investigation of the twister ribozyme

Yijin Liu, Timothy J. Wilson, Scott A. McPhee, David M. J. Lilley (Lead / Corresponding author)

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    63 Citations (Scopus)

    Abstract

    We present a crystal structure at 2.3-Å resolution of the recently described nucleolytic ribozyme twister. The RNA adopts a previously uncharacterized compact fold based on a double-pseudoknot structure, with the active site at its center. Eight highly conserved nucleobases stabilize the core of the ribozyme through the formation of one Watson-Crick and three noncanonical base pairs, and the highly conserved adenine 3' of the scissile phosphate is bound in the major groove of an adjacent pseudoknot. A strongly conserved guanine nucleobase directs its Watson-Crick edge toward the scissile phosphate in the crystal structure, and mechanistic evidence supports a role for this guanine as either a general base or acid in a concerted, general acid-base-catalyzed cleavage reaction.
    Original languageEnglish
    Pages (from-to)739-744
    Number of pages6
    JournalNature Chemical Biology
    Volume10
    Issue number9
    DOIs
    Publication statusPublished - Sep 2014

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    Catalytic RNA
    Guanine
    Phosphates
    Acids
    Adenine
    Base Pairing
    Catalytic Domain
    RNA

    Cite this

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    title = "Crystal structure and mechanistic investigation of the twister ribozyme",
    abstract = "We present a crystal structure at 2.3-{\AA} resolution of the recently described nucleolytic ribozyme twister. The RNA adopts a previously uncharacterized compact fold based on a double-pseudoknot structure, with the active site at its center. Eight highly conserved nucleobases stabilize the core of the ribozyme through the formation of one Watson-Crick and three noncanonical base pairs, and the highly conserved adenine 3' of the scissile phosphate is bound in the major groove of an adjacent pseudoknot. A strongly conserved guanine nucleobase directs its Watson-Crick edge toward the scissile phosphate in the crystal structure, and mechanistic evidence supports a role for this guanine as either a general base or acid in a concerted, general acid-base-catalyzed cleavage reaction.",
    author = "Yijin Liu and Wilson, {Timothy J.} and McPhee, {Scott A.} and Lilley, {David M. J.}",
    year = "2014",
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    TY - JOUR

    T1 - Crystal structure and mechanistic investigation of the twister ribozyme

    AU - Liu, Yijin

    AU - Wilson, Timothy J.

    AU - McPhee, Scott A.

    AU - Lilley, David M. J.

    PY - 2014/9

    Y1 - 2014/9

    N2 - We present a crystal structure at 2.3-Å resolution of the recently described nucleolytic ribozyme twister. The RNA adopts a previously uncharacterized compact fold based on a double-pseudoknot structure, with the active site at its center. Eight highly conserved nucleobases stabilize the core of the ribozyme through the formation of one Watson-Crick and three noncanonical base pairs, and the highly conserved adenine 3' of the scissile phosphate is bound in the major groove of an adjacent pseudoknot. A strongly conserved guanine nucleobase directs its Watson-Crick edge toward the scissile phosphate in the crystal structure, and mechanistic evidence supports a role for this guanine as either a general base or acid in a concerted, general acid-base-catalyzed cleavage reaction.

    AB - We present a crystal structure at 2.3-Å resolution of the recently described nucleolytic ribozyme twister. The RNA adopts a previously uncharacterized compact fold based on a double-pseudoknot structure, with the active site at its center. Eight highly conserved nucleobases stabilize the core of the ribozyme through the formation of one Watson-Crick and three noncanonical base pairs, and the highly conserved adenine 3' of the scissile phosphate is bound in the major groove of an adjacent pseudoknot. A strongly conserved guanine nucleobase directs its Watson-Crick edge toward the scissile phosphate in the crystal structure, and mechanistic evidence supports a role for this guanine as either a general base or acid in a concerted, general acid-base-catalyzed cleavage reaction.

    U2 - 10.1038/nchembio.1587

    DO - 10.1038/nchembio.1587

    M3 - Article

    C2 - 25038788

    VL - 10

    SP - 739

    EP - 744

    JO - Nature Chemical Biology

    JF - Nature Chemical Biology

    SN - 1552-4450

    IS - 9

    ER -