2INC: Native Toluene/o-xylene Monooxygenase Hydroxylase X-ray Crystal Structure

We report the X-ray crystal structures of native and manganese(II)-reconstituted toluene/o-xylene monooxygenase hydroxylase (ToMOH) from Pseudomonas stutzeri OX1 to 1.85 and 2.20 A resolution, respectively. The structures reveal that reduction of the dimetallic active site is accompanied by a carboxylate shift and alteration of the coordination environment for dioxygen binding and activation. A rotamer shift in a strategically placed asparagine 202 accompanies dimetallic center reduction and is proposed to influence protein component interactions. This rotamer shift is conserved between ToMOH and the corresponding residue in methane monooxygenase hydroxylase (MMOH). Previously unidentified hydrophobic pockets similar to those present in MMOH are assigned.
PDB ID: 2INCDownload
MMDB ID: 42975
PDB Deposition Date: 2006/10/6
Updated in MMDB: 2006/12
Experimental Method:
x-ray diffraction
Resolution: 1.85  Å
Source Organism:
Similar Structures:
Biological Unit for 2INC: hexameric; determined by author
Molecular Components in 2INC
Label Count Molecule
Proteins (6 molecules)
Toluene, O-xylene Monooxygenase Oxygenase Subunit
Molecule annotation
Toluene, O-xylene Monooxygenase Oxygenase Subunit
Molecule annotation
Toub Protein
Molecule annotation
Chemicals (6 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB