Cloned (Comment) | Organism |
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- |
Pseudomonas mendocina |
Crystallization (Comment) | Organism |
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structures of toluene 4-monooxygenase hydroxylase in complex with reaction products and effector protein. Active site residue F176 traps the aromatic ring of products against a surface of the active site cavity formed by G103, E104 and A107, while F196 positions the aromatic ring against this surface via a pi-stacking interaction. Effector protein binding produces significant shifts in the positions of residues along the outer portion of the active site (T201, N202, and Q228) and in some iron ligands (E231 and E197), but minor shifts ae produced in F176, F196, and other interior residues of the active site | Pseudomonas mendocina |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas mendocina | Q00456 and Q00457 and Q00460 and Q00459 | Q00456, Q00457 an Q00460 are components TmoA, TmoB and TmoE of diiron hydroxylase T4MOH, respectively, Q00459 i.e. effector protein T4MOD | - |
Pseudomonas mendocina KR1 | Q00456 and Q00457 and Q00460 and Q00459 | Q00456, Q00457 an Q00460 are components TmoA, TmoB and TmoE of diiron hydroxylase T4MOH, respectively, Q00459 i.e. effector protein T4MOD | - |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
iron-sulfur centre | complexes with phenolic products yield an asymmetric my-phenoxo-bridged diiron center and a shift of diiron ligand E231 into a hydrogen bonding position with conserved residue T201 | Pseudomonas mendocina |