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Structural basis for mRNA recognition by elongation factor SelB.

Abstract：

:In bacteria, incorporation of selenocysteine, the 21(st) amino acid, into proteins requires elongation factor SelB, which has the unusual property of binding to both transfer RNA (tRNA) and mRNA. SelB binds to an mRNA hairpin formed by the selenocysteine insertion sequence (SECIS) with extremely high specificity, the molecular basis of which has been unknown. We have determined the crystal structure of the mRNA-binding domain of SelB in complex with SECIS RNA at a resolution of 2.3 A. This is the first example of a complex between an RNA and a winged-helix (WH) domain, a motif found in many DNA-binding proteins and recently discovered in RNA-binding proteins. Notably, RNA binding does not induce a major conformational change in the WH motif. The structure reveals a new mode of RNA recognition with a geometry that allows the complex to wrap around the small ribosomal subunit.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Yoshizawa S,Rasubala L,Ose T,Kohda D,Fourmy D,Maenaka K

doi

10.1038/nsmb890

keywords:

subject

Has Abstract

pub_date

2005-02-01 00:00:00

pages

198-203

issue

2

eissn

1545-9993

issn

1545-9985

pii

nsmb890

journal_volume

12

pub_type

杂志文章

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