3TUP

Crystal structure of human mitochondrial PheRS complexed with tRNAPhe in the active open state

3TUP の概要

• エントリーDOI: 10.2210/pdb3tup/pdb
• 関連するPDBエントリー: 1PYS 3CMQ
• 分子名称: Phenylalanyl-tRNA synthetase, mitochondrial, Thermus thermophilus tRNAPhe (2 entities in total)
• 機能のキーワード: class ii aars, rrm fold, aminoacylation, mitochondria, ligase-rna complex, ligase/rna
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Mitochondrion matrix (Potential): O95363
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72992.57

構造登録者

Safro, M.,Klipcan, L.,Moor, N.,Finarov, I.,Kessler, N.,Sukhanova, M. (登録日: 2011-09-17, 公開日: 2011-11-23, 最終更新日: 2024-02-28)

主引用文献

Klipcan, L.,Moor, N.,Finarov, I.,Kessler, N.,Sukhanova, M.,Safro, M.G.
Crystal Structure of Human Mitochondrial PheRS Complexed with tRNA(Phe) in the Active "Open" State.
J.Mol.Biol., 415:527-537, 2012

PubMed Abstract: Monomeric human mitochondrial phenylalanyl-tRNA synthetase (PheRS), or hmPheRS, is the smallest known enzyme exhibiting aminoacylation activity. HmPheRS consists of only two structural domains and differs markedly from heterodimeric eukaryotic cytosolic and bacterial analogs both in the domain organization and in the mode of tRNA binding. Here, we describe the first crystal structure of mitochondrial aminoacyl-tRNA synthetase (aaRS) complexed with tRNA at a resolution of 3.0 Å. Unlike bacterial PheRSs, the hmPheRS recognizes C74, the G1-C72 base pair, and the "discriminator" base A73, proposed to contribute to tRNA(Phe) identity in the yeast mitochondrial enzyme. An interaction of the tRNA acceptor stem with the signature motif 2 residues of hmPheRS is of critical importance for the stabilization of the CCA-extended conformation and its correct placement in the synthetic site of the enzyme. The crystal structure of hmPheRS-tRNA(Phe) provides direct evidence that the formation of the complex with tRNA requires a significant rearrangement of the anticodon-binding domain from the "closed" to the productive "open" state. Global repositioning of the domain is tRNA modulated and governed by long-range electrostatic interactions.

PubMed: 22137894
DOI: 10.1016/j.jmb.2011.11.029

実験手法

X-RAY DIFFRACTION (3.05 Å)