Summary information and primary citation
- PDB-id
-
1wsu;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- translation-RNA
- Method
- X-ray (2.3 Å)
- Summary
- C-terminal domain of elongation factor selb complexed
with secis RNA
- Reference
-
Yoshizawa S, Rasubala L, Ose T, Kohda D, Fourmy D,
Maenaka K (2005): "Structural
basis for mRNA recognition by elongation factor
SelB." Nat.Struct.Mol.Biol.,
12, 198-203. doi: 10.1038/nsmb890.
- 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.
