EC Number   |
Subunits |
Reference |
|---|
    2.7.7.23 | dimer |
1 * 64000 + 1 * 57000 |
643069 |
| 2.7.7.23 | dimer |
2 * 33000, SDS-PAGE, gel filtration |
643067 |
| 2.7.7.23 | dimer |
2 * 64000, SDS-PAGE, gel filtration |
643065 |
| 2.7.7.23 | hexamer |
trimer/hexamer equilibrium, sedimentation equilibrium analytical ultracentrifugation. Two trimers assemble through their N-terminal domains. The interaction is mediated by a loop that undergoes a large conformational change in the uridyl transferase reaction |
723724 |
| 2.7.7.23 | monomer |
1 * 50000, SDS-PAGE, 1 * 49624, calculated from the deduced amino acid sequence, native mass by gel filtration |
662429 |
| 2.7.7.23 | monomer |
1 * 58300, SDS-PAGE |
721526 |
| 2.7.7.23 | More |
C324 does not form a disulphide bond with any other cysteine. This is consistent with the replacement of C307 by a serine in Y. pestis and the great distance between the three other cysteines (C296, C301 and C385) and C324 |
-, 735569 |
| 2.7.7.23 | More |
the enzyme contains the the N-terminal nucleotidylyltransferase domain (residues 1210) and the C-terminal acetyltransferase domain (residues 211401), respectively. Comparisons of the crystal structures of the ST0452 protein, PDB ID GGO, and Escherichia coli protein EcGlmU2, PDB ID 2OI5, comparison with ST0452 mutant enzymes, overview. Despite the structural similarities between the N- and C-termini of the ST0452 protein and those of Escherichia coli EcGlmU, the thermostabilities of the two proteins differ greatly, as EcGlmU is a mesophilic enzyme. The structures of these proteins do not correlate directly with their thermostability |
-, 729696 |
| 2.7.7.23 | trimer |
- |
643073, 643075, 643076 |
| 2.7.7.23 | trimer |
3 * 50100, SDS-PAGE, gel filtration, all truncated forms form trimers except Tr250 (monomer) |
-, 288688 |
