2pid
From Proteopedia
Crystal structure of human mitochondrial tyrosyl-tRNA synthetase in complex with an adenylate analog
Overview
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.
About this Structure
2PID is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human mitochondrial tyrosyl-tRNA synthetase reveals common and idiosyncratic features., Bonnefond L, Frugier M, Touze E, Lorber B, Florentz C, Giege R, Sauter C, Rudinger-Thirion J, Structure. 2007 Nov;15(11):1505-16. PMID:17997975 Page seeded by OCA on Sun May 4 13:10:07 2008
Categories: Homo sapiens | Single protein | Tyrosine--tRNA ligase | Bonnefond, L. | Florentz, C. | Frugier, M. | Giege, R. | Lorber, B. | Rudinger-Thirion, J. | Sauter, C. | Touze, E. | Aminoacyl-trna synthetase | Atp-binding | Ligase | Mitochondrion | Nucleotide-binding | Protein biosynthesis | Protein-substrate complex
