EC Number   |
Subunits |
Reference |
|---|
    1.8.4.9 | tetramer |
- |
669891 |
| 1.8.4.9 | dimer |
2 * 46000, SDS-PAGE |
689431 |
| 1.8.4.9 | heterotetramer |
2 * 75000 + 2 * 20000 |
667717 |
| 1.8.4.9 | dimer |
alpha2, 2 * 43000, comparison of native mass after gel filtration with denatured after SDS-PAGE |
288644 |
| 1.8.4.9 | More |
amino acid residues 73-327 form the R-domain which is homologous to microbial 5'-phosphoadenylylsulfate reductase, and of residues 328-465 form the C-domain which is homologous to thioredoxin, the domains alone are inactive, but mixing of both can partially rstore activity |
660399 |
| 1.8.4.9 | More |
the recombinant detagged monomeric form of the AtAPR1 redox domain has 13 kDa measured by SDS-PAGE. Because plant APR1 is arranged as oligomers, this result implies that the oligomerization of AtAPR1 is not formed via redox domain self-interaction. The structure of the AtAPR1 redox domain is a compact spherical molecule comprising a central core of five-stranded beta-sheets flanked on either side by four helices. The fold of the redox domain arranged in the order beta1-alpha1-beta2-alpha2-beta3-alpha3-beta4-beta5-alpha4 is similar to the thioredoxin fold but not glutaredoxin fold. The N-terminal region begins with a short beta1 strand (residues Val4-Leu6), followed by alpha1 and beta2, consisting of residues Arg8 to Lys16 and Trp24 to Tyr29, respectively. The redox-active motif (Cys33-Pro34-Phe35-Cys36) is located at the N-terminal end of the alpha2-helix, consisting of residues Pro34 to Leu50. The strand beta3 comprises residues Lys56 to Arg61, followed by beta4 (Thr81-Phe85), beta5 (Ile93-Tyr95) and a C-terminal helix which consists of residues Lys99 to Glu111. Strands beta1, beta2, and beta3 are parallel, and strand beta4 is antiparallel to beta2 and beta5. Helices alpha1 and alpha3 pack on one side of the central beta-sheet, whereas helices alpha2 and alpha4 are located at opposite sides. The packing of the sandwich-like architecture is mainly maintained by hydrophobic interactions between the sheet and helices. Surface potential distribution of the redox domain shows most positive-charged residues around the redox-active motif |
763921 |
| 1.8.4.9 | ? |
x * 29000, recombinant enzyme, SDS-PAGE |
660168 |
| 1.8.4.9 | ? |
x * 32000, SDS-PAGE |
687585 |
| 1.8.4.9 | ? |
x * 50000, recombinant His-tagged PpAPR, SDS-PAGE |
687585 |
