1ckv
From Proteopedia
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STRUCTURE OF THE SOLUBLE METHANE MONOOXYGENASE REGULATORY PROTEIN B
Overview
The soluble methane monooxygenase (sMMO; EC 1.14.13.25) from the, pseudothermophile Methylococcus capsulatus (Bath) is a three-component, enzyme system that catalyzes the selective oxidation of methane to, methanol. We have used NMR spectroscopy to produce a highly refined, structure of MMOB, the 16-kDa regulatory protein of this system. This, structure has a unique and intricate fold containing seven beta-strands, forming two beta-sheets oriented perpendicular to each other and bridged, by three alpha-helices. The rate and efficiency of the methane, hydroxylation by sMMO depend on dynamic binding interactions of the, hydroxylase with the reductase and regulatory protein components during, catalysis. We have monitored by NMR the binding of MMOB to the hydroxylase, in the presence and absence of the reductase. The results of these studies, provide structural insight into how the regulatory protein interacts with, the hydroxylase.
About this Structure
1CKV is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of the soluble methane monooxygenase regulatory protein B., Walters KJ, Gassner GT, Lippard SJ, Wagner G, Proc Natl Acad Sci U S A. 1999 Jul 6;96(14):7877-82. PMID:10393915
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