1PYB

Crystal Structure of Aquifex aeolicus Trbp111: a Structure-Specific tRNA Binding Protein

1PYB の概要

• エントリーDOI: 10.2210/pdb1pyb/pdb
• 関連するPDBエントリー: 1PXF
• 分子名称: tRNA-binding protein Trbp111 (2 entities in total)
• 機能のキーワード: oligonucleotide, oligosaccharide-binding fold, ob-fold, beta-barrel, rna binding protein
• 由来する生物種: Aquifex aeolicus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 48448.53

構造登録者

Swairjo, M.A.,Morales, A.J.,Wang, C.C.,Ortiz, A.R.,Schimmel, P. (登録日: 2003-07-08, 公開日: 2003-08-05, 最終更新日: 2023-08-16)

主引用文献

Swairjo, M.A.,Morales, A.J.,Wang, C.C.,Ortiz, A.R.,Schimmel, P.
Crystal structure of trbp111: a structure-specific tRNA-binding protein.
Embo J., 19:6287-6298, 2000

PubMed Abstract: 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 A, 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 ss-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 ss-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.

PubMed: 11101501
DOI: 10.1093/emboj/19.23.6287

実験手法

X-RAY DIFFRACTION (2.5 Å)