2IND
Mn(II) Reconstituted Toluene/o-xylene Monooxygenase Hydroxylase X-ray Crystal Structure
Summary for 2IND
| Entry DOI | 10.2210/pdb2ind/pdb |
| Related | 1T0Q |
| Descriptor | Toluene, o-xylene monooxygenase oxygenase subunit, TouB protein, MANGANESE (II) ION, ... (6 entities in total) |
| Functional Keywords | manganese reconstitution, 4-helix bundle, carboxylate bridge, metalloenzyme, oxidoreductase |
| Biological source | Pseudomonas stutzeri More |
| Total number of polymer chains | 3 |
| Total formula weight | 104653.24 |
| Authors | McCormick, M.S.,Sazinsky, M.H.,Condon, K.L.,Lippard, S.J. (deposition date: 2006-10-06, release date: 2006-12-05, Last modification date: 2023-08-30) |
| Primary citation | McCormick, M.S.,Sazinsky, M.H.,Condon, K.L.,Lippard, S.J. X-ray crystal structures of manganese(II)-reconstituted and native toluene/o-xylene monooxygenase hydroxylase reveal rotamer shifts in conserved residues and an enhanced view of the protein interior. J.Am.Chem.Soc., 128:15108-15110, 2006 Cited by PubMed Abstract: 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. PubMed: 17117860DOI: 10.1021/ja064837r PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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