EC Number   |
Subunits |
Reference |
|---|
   2.7.7.79 | ? |
x * 18000, SDS-PAGE |
-, 761202 |
| 2.7.7.79 | ? |
x * 25000, SDS-PAGE |
-, 761202 |
| 2.7.7.79 | ? |
x * 28000, calculated from sequence |
712106 |
| 2.7.7.79 | ? |
x * 30000, SDS-PAGE |
712106 |
| 2.7.7.79 | dimer |
2 * 58000, SDS-PAGE |
712335 |
| 2.7.7.79 | dimer |
Methanosarcina acetivorans TLP forms a dimer coordinating on tRNA. While the dimer binds the acceptor stem and T arm of its tRNA substrate, the anticodon loop is not coordinated by TLP enzymes |
761202 |
| 2.7.7.79 | More |
crystal structures of eukaryotic Thg1 enzymes shows that monomeric Thg1 is composed of a six-strand antiparallel beta-sheet flanked by three or four alpha-helices on each side, along with a protruding long arm composed of two antiparallel beta-strands. Each monomer forms a dimer, mediated by salt bridge formation and hydrogen bonding between the beta-sheet and an alpha-helix. Alanine scanning mutagenesis in Saccharomyces cerevisiae Thg1 (ScThg1) of conserved residues responsible for mediating dimer formation has shown strongly diminished G-1 addition activity. Dimer-of-dimer formation stems from initial dimer formation., the alpha-helix of the N-terminus in monomer A interacts with the nucleotide binding site of monomer B and ultimately forms an intertwined N-terminus segment, which again interacts with a symmetrical dimer to form its active tetrameric form. Eukaryotic Thg1 enzymes show monomeric Thg1 that is composed of a six-strand antiparallel beta-sheet flanked by three or four alpha-helices on each side, along with a protruding long arm composed of two antiparallel beta-strands. Structure-function analyses of Thg1 and TLP enzymes, overview |
-, 761202 |
| 2.7.7.79 | More |
eukaryotic Thg1 enzymes show monomeric Thg1 that is composed of a six-strand antiparallel beta-sheet flanked by three or four alpha-helices on each side, along with a protruding long arm composed of two antiparallel beta-strands |
761202 |
| 2.7.7.79 | More |
eukaryotic Thg1 enzymes show monomeric Thg1 that is composed of a six-strand antiparallel beta-sheet flanked by three or four alpha-helices on each side, along with a protruding long arm composed of two antiparallel beta-strands. Structure-function analyses of Thg1 and TLP enzymes, overview |
-, 761202 |
| 2.7.7.79 | tetramer |
4 * 27800, about, sequence calculation and crystal structure |
-, 760482 |
