Table 2.
Functionally important residues in MmoX vs. IsoA, mapped according to Methylosinus trichosporium Ob3b (MmoX) and Rhodococcus sp. AD45 (IsoA) sequence numbering. Note: The functional roles of IsoA residues are putative, based solely on in silico structural and sequence homology with MmoX (PDB 1MTY). These predicted correspondences identify candidate positions for future site-directed mutagenesis to verify catalytic and structural roles within the IsoMO di-iron centre.
| Residue function | MmoX | IsoA |
|---|---|---|
| Gating | L110 | L101 |
| Enantioselectivity | G113, G208 | G104, V202 |
| Important in methane oxidation | C151, M184, F282 | D147, V178, F274 |
| Highly conserved | T213 | T207 |
| Iron ligand | E114, E144, H147, E209, E243, H246 | E110, E140, H143, E203, E237, H240 |
| Hydrogen bonding between C and F helices | D143, R146, S238, D242, R245 | D139, R142, S232, D236, R239 |
| Access of substrates and release of products to and from the active site | T213, N214, E240 | T207, N208, Q234 |
| Tightly packed regions of the protein | A117, G250 | A113, G244 |
| Canyon | Y67, K74, L321, G325, P329 | Y64, K71, G315, P319 |
| Handle | A224, G228, D229 | A218, G222, D223 |
| Possible docking | Y292, W371, Y376, P377 | Y284, W362, Y367, P368 |
| Interact with gamma | P424, G443, P461, Y464 | P408, G427, Y430 |