Journal
EMBO JOURNAL
Volume 19, Issue 23, Pages 6287-6298Publisher
OXFORD UNIV PRESS
DOI: 10.1093/emboj/19.23.6287
Keywords
stal structure; oligonucleotide; oligosaccharide-binding fold; RNA binding protein; tRNA synthetase
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Funding
- NIGMS NIH HHS [R01 GM015539, R01 GM023562, GM15539, GM23562] Funding Source: Medline
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Trbp111 is a 111 amino acid Aquifex aeolicus structure-specific tRNA-binding protein that has homologous counterparts distributed throughout evolution. A dimer is the functional unit for binding a single tRNA. Here we report the 3D structures of the A.aeolicus protein and its Escherichia coli homolog at resolutions of 2.50 and 1.87 Angstrom, respectively. The structure shows a symmetrical dimer of two core domains and a central dimerization domain where the N- and C-terminal regions of Trbp111 form an extensive dimer interface, The core of the monomer is a classical oligonucleotide/oligosaccharide-binding (OB) fold with a five-stranded beta -barrel and a small capping helix. This structure is similar to that seen in the anticodon-binding domain of three class II tRNA synthetases and several other proteins. Mutational analysis identified sites important for interactions with tRNA. These residues line the inner surfaces of two clefts formed between the beta -barrel of each monomer and the dimer interface. The results are consistent with a proposed model for asymmetrical docking of the convex side of tRNA to the dimer.
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