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2inc

From Proteopedia

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{{STRUCTURE_2inc| PDB=2inc | SCENE= }}
{{STRUCTURE_2inc| PDB=2inc | SCENE= }}
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'''Native Toluene/o-xylene Monooxygenase Hydroxylase X-ray Crystal Structure'''
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===Native Toluene/o-xylene Monooxygenase Hydroxylase X-ray Crystal Structure===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_17117860}}
==About this Structure==
==About this Structure==
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[[Category: Diiron]]
[[Category: Diiron]]
[[Category: Metalloenzyme]]
[[Category: Metalloenzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:41:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:21:09 2008''

Revision as of 19:21, 27 July 2008

Image:2inc.png

Template:STRUCTURE 2inc

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

Template:ABSTRACT PUBMED 17117860

About this Structure

2INC is a Protein complex structure of sequences from Pseudomonas stutzeri. 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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