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1WSU

C-terminal domain of elongation factor selB complexed with SECIS RNA

Summary for 1WSU
Entry DOI10.2210/pdb1wsu/pdb
Descriptor5'-R(*GP*GP*CP*GP*UP*UP*GP*CP*CP*GP*GP*UP*CP*U*GP*GP*CP*AP*AP*CP*GP*CP*C)-3', Selenocysteine-specific elongation factor (3 entities in total)
Functional Keywordswinged-helix, translation-rna complex, translation/rna
Biological sourceMoorella thermoacetica
More
Cellular locationCytoplasm: Q46455
Total number of polymer chains7
Total formula weight79128.05
Authors
Yoshizawa, S.,Rasubala, L.,Ose, T.,Kohda, D.,Fourmy, D.,Maenaka, K. (deposition date: 2004-11-11, release date: 2005-01-25, Last modification date: 2023-10-25)
Primary citationYoshizawa, S.,Rasubala, L.,Ose, T.,Kohda, D.,Fourmy, D.,Maenaka, K.
Structural basis for mRNA recognition by elongation factor SelB
Nat.Struct.Mol.Biol., 12:198-203, 2005
Cited by
PubMed 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.
PubMed: 15665870
DOI: 10.1038/nsmb890
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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数据于2024-11-06公开中

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