PDBsum entry 2ind

Oxidoreductase

PDB id: 2ind

Contents

Protein chains

491 a.a.

323 a.a.

83 a.a.

Ligands

P6G

Metals

_MN ×2

Waters ×141

References listed in PDB file

Key reference

• Title: 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.
• Authors: M.S.Mccormick, M.H.Sazinsky, K.L.Condon, S.J.Lippard.
• Ref.: J Am Chem Soc, 2006, 128, 15108-15110.
• PubMed id: 17117860

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.