2ply

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Revision as of 10:22, 23 January 2008

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spinqualitylabelsall models 2ply, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure of the mRNA binding fragment of elongation factor SelB in complex with SECIS RNA.

Overview

Elongation factor SelB is responsible for co-translational incorporation, of selenocysteine (Sec) into proteins. The UGA stop codon is recoded as a, Sec codon in the presence of a downstream mRNA hairpin. In prokaryotes, in, addition to the EF-Tu-like N-terminal domains, a C-terminal extension, containing four tandem winged-helix motifs (WH1-4) recognizes the mRNA, hairpin. The 2.3-A resolution crystal structure of the Escherichia coli, WH3/4 domains bound to mRNA with mutagenesis data reveal that the two WH, motifs use the same structural elements to bind RNA. The structure, together with the 2.6-A resolution structure of the WH1-4 domains from, Moorella thermoacetica bound to RNA revealed that a salt bridge connecting, WH2 to WH3 modules is disrupted upon mRNA binding. The results provide a, structural basis for the molecular switch that may allow communication, between tRNA and mRNA binding sites and illustrate how RNA acts as an, activator of the switch. The structures show that tandem WH motifs not, only provide an excellent scaffold for RNA binding but can also have an, active role in the function of protein-RNA complexes.

About this Structure

2PLY is a Protein complex structure of sequences from Moorella thermoacetica with , , and as ligands. Full crystallographic information is available from OCA.

Reference

Structural insight into a molecular switch in tandem winged-helix motifs from elongation factor SelB., Soler N, Fourmy D, Yoshizawa S, J Mol Biol. 2007 Jul 20;370(4):728-41. Epub 2007 May 10. PMID:17537456

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