2pid
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | We report the structure of a strictly mitochondrial human synthetase, namely tyrosyl-tRNA synthetase (mt-TyrRS), in complex with an adenylate | + | 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== | ==About this Structure== | ||
| Line 10: | Line 10: | ||
==Reference== | ==Reference== | ||
| - | Crystal | + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17997975 17997975] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 31: | Line 31: | ||
[[Category: protein-substrate complex]] | [[Category: protein-substrate complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:29:43 2008'' |
Revision as of 16:29, 21 February 2008
|
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 with as ligand. Active as Tyrosine--tRNA ligase, with EC number 6.1.1.1 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 Thu Feb 21 18:29:43 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. | YSA | Aminoacyl-trna synthetase | Atp-binding | Ligase | Mitochondrion | Nucleotide-binding | Protein biosynthesis | Protein-substrate complex
