3DHG
Crystal Structure of Toluene 4-Monoxygenase Hydroxylase
Summary for 3DHG
| Entry DOI | 10.2210/pdb3dhg/pdb |
| Descriptor | toluene 4-monooxygenase hydroxylase alpha subunit, toluene 4-monooxygenase hydroxylase beta subunit, toluene 4-monooxygenase hydroxylase gamma subunit, ... (7 entities in total) |
| Functional Keywords | multicomponent monooxygenase, aromatic hydrocarbons catabolism, fad, flavoprotein, iron, monooxygenase, oxidoreductase |
| Biological source | Pseudomonas mendocina More |
| Total number of polymer chains | 6 |
| Total formula weight | 212951.23 |
| Authors | Bailey, L.J.,Mccoy, J.G.,Phillips Jr., G.N.,Fox, B.G. (deposition date: 2008-06-17, release date: 2008-12-30, Last modification date: 2024-02-21) |
| Primary citation | Bailey, L.J.,McCoy, J.G.,Phillips Jr., G.N.,Fox, B.G. Structural consequences of effector protein complex formation in a diiron hydroxylase. Proc.Natl.Acad.Sci.USA, 105:19194-19198, 2008 Cited by PubMed Abstract: Carboxylate-bridged diiron hydroxylases are multicomponent enzyme complexes responsible for the catabolism of a wide range of hydrocarbons and as such have drawn attention for their mechanism of action and potential uses in bioremediation and enzymatic synthesis. These enzyme complexes use a small molecular weight effector protein to modulate the function of the hydroxylase. However, the origin of these functional changes is poorly understood. Here, we report the structures of the biologically relevant effector protein-hydroxylase complex of toluene 4-monooxygenase in 2 redox states. The structures reveal a number of coordinated changes that occur up to 25 A from the active site and poise the diiron center for catalysis. The results provide a structural basis for the changes observed in a number of the measurable properties associated with effector protein binding. This description provides insight into the functional role of effector protein binding in all carboxylate-bridged diiron hydroxylases. PubMed: 19033467DOI: 10.1073/pnas.0807948105 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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