2PID

Crystal structure of human mitochondrial tyrosyl-tRNA synthetase in complex with an adenylate analog

2PID の概要

• エントリーDOI: 10.2210/pdb2pid/pdb
• 関連するPDBエントリー: 1vbm 3ts1
• 分子名称: Tyrosyl-tRNA synthetase, 5'-O-[N-(L-TYROSYL)SULFAMOYL]ADENOSINE (3 entities in total)
• 機能のキーワード: aminoacyl-trna synthetase, protein-substrate complex, atp-binding, ligase, mitochondrion, nucleotide-binding, protein biosynthesis
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Mitochondrion matrix: Q9Y2Z4
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 80943.73

構造登録者

Bonnefond, L.,Frugier, M.,Touze, E.,Lorber, B.,Florentz, C.,Giege, R.,Sauter, C.,Rudinger-Thirion, J. (登録日: 2007-04-13, 公開日: 2007-10-23, 最終更新日: 2024-03-13)

主引用文献

Bonnefond, L.,Frugier, M.,Touze, E.,Lorber, B.,Florentz, C.,Giege, R.,Sauter, C.,Rudinger-Thirion, J.
Crystal Structure of Human Mitochondrial Tyrosyl-tRNA Synthetase Reveals Common and Idiosyncratic Features.
Structure, 15:1505-1516, 2007

PubMed Abstract: We report the structure of a strictly mitochondrial human synthetase, namely tyrosyl-tRNA synthetase (mt-TyrRS), in complex with an adenylate analog at 2.2 A resolution. The structure is that of an active enzyme deprived of the C-terminal S4-like domain and resembles eubacterial TyrRSs with a canonical tyrosine-binding pocket and adenylate-binding residues typical of class I synthetases. Two bulges at the enzyme surface, not seen in eubacterial TyrRSs, correspond to conserved sequences in mt-TyrRSs. The synthetase electrostatic surface potential differs from that of other TyrRSs, including the human cytoplasmic homolog and the mitochondrial one from Neurospora crassa. The homodimeric human mt-TyrRS shows an asymmetry propagating from the dimer interface toward the two catalytic sites and extremities of each subunit. Mutagenesis of the catalytic domain reveals functional importance of Ser200 in line with an involvement of A73 rather than N1-N72 in tyrosine identity.

PubMed: 17997975
DOI: 10.1016/j.str.2007.09.018

実験手法

X-RAY DIFFRACTION (2.2 Å)