Crystallization (Comment) | Organism |
---|---|
purified mitochondrial PheRS complexed with Phe-AMP, cryoprotection by mother liquor solution containing 25% glycerol, X-ray diffraction structure determination and analysis at 2.2 A resolution | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | mitochondrial PheRS is nuclear-encoded | Homo sapiens | 5739 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Homo sapiens |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
45000 | - |
mitPheRS, gel filtration | Homo sapiens |
49600 | - |
1 * 49600, sequence calculation | Homo sapiens |
71000 | - |
binary mitPheRS-tRNAPhe complex, gel filtration | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-phenylalanine + tRNAPhe | Homo sapiens | - |
AMP + diphosphate + L-phenylalanyl-tRNAPhe | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-phenylalanine + tRNAPhe | - |
Homo sapiens | AMP + diphosphate + L-phenylalanyl-tRNAPhe | - |
? | |
ATP + L-phenylalanine + tRNAPhe | recognition of phenylalanyl-adenylate and substrate binding structure, docking model, overview. Formation of the PheRS-tRNAPhe complex in human mitochondria must be accompanied by considerable rearrangement, i.e. hinge-type rotation through about 160degree, of the anticodon binding domain upon tRNA binding, overview | Homo sapiens | AMP + diphosphate + L-phenylalanyl-tRNAPhe | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 49600, sequence calculation | Homo sapiens |
More | human mitPheRS consists of four major parts: the N-terminal region, residues 1-47, the catalytic domain, residues 48-289, the linker region, residues 290-322, and the C-terminal domain, residues 323-415. Multimeric organization is not a prerequisite for phenylalanylation activity, as monomeric mitochondrial phenylalanyl-tRNA synthetase is also active. The anticodon binding domain of the beta subunit of alphabeta2 PheRS is located at the C-terminus of mitPheRS overlapping with the acceptor stem of phenylalanine transfer RNA, structure, overview | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
mitochondrial phenylalanyl-tRNA synthetase | - |
Homo sapiens |
mitochondrial PheRS | - |
Homo sapiens |
mitPheRS | - |
Homo sapiens |
Phenylalanyl-tRNA synthetase | - |
Homo sapiens |
PheRS | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Homo sapiens |