3dhh | pdb_00003dhh
Crystal Structure of Resting State Toluene 4-Monoxygenase Hydroxylase Complexed with Effector Protein
Structural highlights
Function[TMOD_PSEME] Effector protein subunit of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol. Required for optimal efficiency and specificity of the holoenzyme.[1] [2] [3] [TMOB_PSEME] Subunit T4moB of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol.[4] [5] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCarboxylate-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. Structural consequences of effector protein complex formation in a diiron hydroxylase.,Bailey LJ, McCoy JG, Phillips GN Jr, Fox BG Proc Natl Acad Sci U S A. 2008 Dec 9;105(49):19194-8. Epub 2008 Nov 25. PMID:19033467[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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