EC Number | Crystallization (Comment) | Organism |
---|---|---|
6.1.1.20 | PheRS in complex with with cognate tRNAPhe and nonhydrolyzable phenylalanyladenylate analogue PheOH-AMP, hanging-drop vapor-diffusion method, 4°C, 3-5 mg/ml protein ina ratio of 1:2,5 with tRNAPhe in 20 mM imidazole-HCl, pH 7.8, 1 mM MgCl2, 5 mM 2-mercaptoethanol, 1 mM NaN3, 10% saturated ammonium sulfate, and 1 mM PheOH-AMP, slow equilibration against a reservoir solution containing the crystallization buffer and 27% saturated ammonium sulfate, cryoprotection by 30% v/v glycerol, X-ray diffraction structure determination and anaylsis at 3.1 A resolution, modeling | Thermus thermophilus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
6.1.1.20 | PheOH-AMP | L-phenylalaninyl-5'-adenylate, a nonhydrolyzable phenylalanyladenylate analogue, conformational changes in tRNAPhe and the catalytic domain are induced by the PheOH-AMP binding: the motif 2 loop and a helical loop, residues 139-152 of the alpha-subunit, undergo coordinated displacement, Metalpha148 of the helical loop adopts a conformation preventing the 2'-OH group of A76 from approaching the alpha-carbonyl carbon of PheOH-AMP, the unfavorable position of the terminal ribose stems from the absence of the R-carbonyl oxygen in the analogue, overview | Thermus thermophilus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.1.1.20 | Mg2+ | - |
Thermus thermophilus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.1.1.20 | ATP + L-phenylalanine + tRNAPhe | Thermus thermophilus | - |
AMP + diphosphate + L-phenylalanyl-tRNAPhe | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.1.1.20 | Thermus thermophilus | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.1.1.20 | ATP + L-phenylalanine + tRNAPhe | - |
Thermus thermophilus | AMP + diphosphate + L-phenylalanyl-tRNAPhe | - |
? | |
6.1.1.20 | ATP + L-phenylalanine + tRNAPhe | charging of cognate amino acid, conformational changes in tRNAPhe and the catalytic domain are induced by the PheOH-AMP or AMP binding, acceptor arm binding and recognition | Thermus thermophilus | AMP + diphosphate + L-phenylalanyl-tRNAPhe | - |
? | |
6.1.1.20 | additional information | tRNAPhe binding structure determination: CCA end orientation is stabilized by extensive base-specific interactions of A76 and C75 with the protein and by intra-RNA interactions of A73 with adjacent nucleotides, the 4-amino group of the bulged out C75 is trapped by two negatively charged residues of the beta-subunit, Glubeta31 and Aspbeta33, highly conserved in eubacterial PheRSs, the position of the A76 base is stabilized by interactions with HisR212 of motif 2 (universally conserved in PheRSs) and class II-invariant ArgR321 of motif 3, overview | Thermus thermophilus | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
6.1.1.20 | tetramer | (alphabeta)2 heterotetramer | Thermus thermophilus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.1.1.20 | Phenylalanyl-tRNA synthetase | - |
Thermus thermophilus |
6.1.1.20 | PheRS | - |
Thermus thermophilus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.1.1.20 | ATP | - |
Thermus thermophilus |