EC Number   |
Subunits |
Reference |
|---|
   2.4.1.173 | ? |
x * 54200, about, sequence calculation |
-, 736786 |
| 2.4.1.173 | ? |
x * 55900, about, sequence calculation |
-, 736786 |
| 2.4.1.173 | ? |
x * 61800, about, sequence calculation |
-, 736786 |
| 2.4.1.173 | ? |
x * 95000, recombinant GFP-tagged enzyme, SDS-PAGE |
-, 760156 |
| 2.4.1.173 | homodimer |
UGT51 forms a dimer in solution. The dimeric structure of UGT51 has two subunits packed against each other in a parallel fashion and adopts a butterfly shape. The full length of UGT51 contain 1198 amino acids, which can be divided into several domains: pleckstrin homology (PH) domain, GRAM domain and catalytic domain. The PH domain responsible interact with membrane lipids, the GRAM domain is essential for proper protein association with its target membrane, while the catalytic domain is essentiell for synthesis steroid glycosides. Each subunit displays the typical GT-B fold of GTs, comprising two distinct N- and C-terminal Rossman-fold domains having a similar topology and connected by a linker peptide and a long C-terminal helix. The N-terminal domain, a seven-stranded parallel beta-sheet flanked by nine alpha-helices, and the C-terminal domain, a six-stranded beta-sheet surrounded by five alpha-helices, are assumed to bind the aglycone and the nucleotide-sugar donor, respectively. The C-terminal helices alpha7 (residues 1129-1144) and alpha8 (residues 1147-1171) cross and interact with each Rossman-fold domain |
-, 759680 |
