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2inc

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2inc, resolution 1.85Å ()
Ligands: ,
Gene: touA (Pseudomonas stutzeri), touE (Pseudomonas stutzeri), touB (Pseudomonas stutzeri)
Domains: AAMH_A, TmoB, AAMH_B
Related: 1t0q
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

Publication Abstract from PubMed

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.

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., McCormick MS, Sazinsky MH, Condon KL, Lippard SJ, J Am Chem Soc. 2006 Nov 29;128(47):15108-10. PMID:17117860

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

2INC is a 3 chains structure of sequences from Pseudomonas stutzeri. Full crystallographic information is available from OCA.

Reference

  • McCormick MS, Sazinsky MH, Condon KL, Lippard SJ. 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. 2006 Nov 29;128(47):15108-10. PMID:17117860

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