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Crystal structure of trbp111: a structure-specific tRNA-binding protein
M A Swairjo1, A J Morales, C C Wang
1Skaags Institute for Chemical Biology, Department of Molecular Biology and Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
The EMBO Journal
|December 2, 2000
Summary
Aquifex aeolicus Trbp111, a tRNA-binding protein, functions as a dimer. Its 3D structure reveals an oligonucleotide/oligosaccharide-binding fold, crucial for tRNA interaction.
Area of Science:
- Structural biology
- Molecular biology
- Biochemistry
Background:
- Trbp111 is a structure-specific tRNA-binding protein from Aquifex aeolicus.
- Homologous proteins are found across evolutionary history.
- A dimer serves as the functional unit for tRNA binding.
Purpose of the Study:
- To determine the 3D structures of Trbp111 and its E. coli homolog.
- To elucidate the structural basis of tRNA binding.
- To identify key residues involved in tRNA interaction.
Main Methods:
- X-ray crystallography was used to determine the 3D structures at 2.50 Å (A. aeolicus) and 1.87 Å (E. coli).
- Mutational analysis was performed to identify critical residues for tRNA binding.
Main Results:
- The structure reveals a symmetrical dimer with core and dimerization domains.
- The monomer core exhibits an oligonucleotide/oligosaccharide-binding (OB) fold.
- Mutational analysis identified residues lining clefts crucial for tRNA interaction.
Conclusions:
- The Trbp111 dimer structure provides insights into tRNA binding mechanisms.
- The identified residues support a model of asymmetrical tRNA docking.
- The OB fold is conserved in tRNA-binding proteins and synthetases.