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Solution structure of domain 5 of a group II intron ribozyme reveals a new RNA motif.

Abstract：

:Domain 5 (D5) is the central core of group II intron ribozymes. Many base and backbone substituents of this highly conserved hairpin participate in catalysis and are crucial for binding to other intron domains. We report the solution structures of the 34-nucleotide D5 hairpin from the group II intron ai5 gamma in the absence and presence of divalent metal ions. The bulge region of D5 adopts a novel fold, where G26 adopts a syn conformation and flips down into the major groove of helix 1, close to the major groove face of the catalytic AGC triad. The backbone near G26 is kinked, exposing the base plane of the adjacent A-U pair to the solvent and causing bases of the bulge to stack intercalatively. Metal ion titrations reveal strong Mg(2+) binding to a minor groove shelf in the D5 bulge. Another distinct metal ion-binding site is observed along the minor groove side of the catalytic triad, in a manner consistent with metal ion binding in the ribozyme active site.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Sigel RK,Sashital DG,Abramovitz DL,Palmer AG,Butcher SE,Pyle AM

doi

10.1038/nsmb717

keywords:

subject

Has Abstract

pub_date

2004-02-01 00:00:00

pages

187-92

issue

2

eissn

1545-9993

issn

1545-9985

pii

nsmb717

journal_volume

11

pub_type

杂志文章

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