Structure of the soluble methane monooxygenase regulatory protein B

The soluble methane monooxygenase (sMMO; EC 1.14.13.25) from the pseudother mophile 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 intrica te fold containing seven beta-strands forming two beta-sheets oriented perp endicular to each other and bridged by three alpha-helices. The rate and ef ficiency of the methane hydroxylation by sMMO depend on dynamic binding int eractions of the hydroxylase with the reductase and regulatory protein comp onents during catalysis. We have monitored by NMR the binding of MMOB to th e hydroxylase in the presence and absence of the reductase. The results of these studies provide structural insight into how the regulatory protein in teracts with the hydroxylase.