EC Number   |
Subunits |
Reference |
|---|
    2.4.2.3 | ? |
x * 27000, SDS-PAGE |
736524 |
| 2.4.2.3 | ? |
x * 27500, calculated, x * 28000, SDS-PAGE |
721222 |
| 2.4.2.3 | ? |
x * 29000, SDS-PAGE |
-, 638517 |
| 2.4.2.3 | dimer |
isozyme UPP1, the N-terminus of the protein forms a strand-turn-strand structure bracketed by two short helices, structure, overview |
702929 |
| 2.4.2.3 | hexamer |
- |
638534 |
| 2.4.2.3 | hexamer |
6 * 27500 |
638519, 638540 |
| 2.4.2.3 | hexamer |
6 * 30200, calculated from sequence |
-, 726781 |
| 2.4.2.3 | homodimer |
- |
759543 |
| 2.4.2.3 | homodimer |
2 * 27500, calculated from amino acid sequence |
735985 |
| 2.4.2.3 | homodimer |
although the homodimer's conformation of PcUP1 is equivalent to the dimer unit in the typical NP-I subfamily, it is not possible to assemble three PcUP1 dimers into the canonical hexamer as a result of a 16-amino-acid insertion in the sequence of PcUP1. This Phytophthora capsici-specific insert creates an additional secondary structural element, that protrudes into the space that would be occupied by the neighboring dimer of the canonical NP-1 hexamer, thus sterically blocking trimerization of the dimers. Trypanosoma brucei TbUP and human HsUPP1 also harbor hexamer-blocking insertions. The strictly ear-shaped conserved catalytic pocket with positive charge of PcUP1 is located on the monomer-monomer hydrophobic interface |
-, 760136 |
