2ind
From Proteopedia
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Mn(II) Reconstituted Toluene/o-xylene Monooxygenase Hydroxylase X-ray Crystal Structure
Overview
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.
About this Structure
2IND is a Protein complex structure of sequences from Pseudomonas stutzeri with and as ligands. Full crystallographic information is available from OCA.
Reference
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
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