EC Number   |
Subunits |
Reference |
|---|
    1.8.99.5 | ? |
x * 12700, subunit DsrC, claculated |
-, 733771 |
| 1.8.99.5 | heterodimer |
- |
-, 764536 |
| 1.8.99.5 | heterotetramer |
2 * 13400 plus 2 * 28400, SDS-PAGE |
394898 |
| 1.8.99.5 | heterotetramer |
2 * 48000, alpha-subunit, 2 * 48000, beta-subunit, SDS-PAGE and N-terminal sequencing |
394043 |
| 1.8.99.5 | homodimer |
2 * 35000, MalPEG-labelled enzyme, SDS-PAGE |
741814 |
| 1.8.99.5 | homotrimer |
with an unprecedented fold and heme arrangement, three-dimensional structure analysis |
743347 |
| 1.8.99.5 | More |
in the CX15CH motif of heme 8, the extended region between the two cysteine residues forms a loop with a short helical turn, in direct vicinity to another loop harbouring the only non-proline cis peptide in the enzyme, between residues G508 and F509. Its formation might require the essential peptidyl isomerase MccB2, and it is presumed to be a prerequisite for correct folding of the loop in the maturation process of heme 8, which is likely to be attached by the dedicated cytochrome c synthase CcsA1. The structure of the CX15CH heme c binding motif disrupts the general parallel/perpendicular heme stacking sequence, and rotates the heme out of plane, possibly to optimize the interaction with the putative electron donor, the iron-sulfur protein MccC |
743347 |
| 1.8.99.5 | multimer |
2 * 50000, alpha-subunit, + 2 * 45000, beta subunit, + 1-3 * 11000, gamma-subunit. The gamma-subunit seems not to be an integral part of the protein |
-, 394066 |
| 1.8.99.5 | tetramer |
2 * 44200, alpha-subunit, + 2 * 41200, beta-subunit |
734637 |
