1tvc
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FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)
OverviewOverview
Soluble methane monooxygenase (sMMO) catalyzes the hydroxylation of, methane by dioxygen to methanol, the first step in carbon assimilation by, methanotrophs. This multicomponent system transfers electrons from NADH, through a reductase component to the non-heme diiron center in the, hydroxylase where O(2) is activated. The reductase component comprises, three distinct domains, a [2Fe-2S] ferredoxin domain along with FAD- and, NADH-binding domains. We report the solution structure of the reduced 27.6, kDa FAD- and NADH-binding domains (MMOR-FAD) of the reductase from, Methylococcus capsulatus (Bath). The FAD-binding domain consists of a, six-stranded antiparallel beta-barrel and one alpha-helix, with the first, 10 N-terminal residues unstructured. In the interface between the two, domains, the FAD cofactor is tightly bound in an unprecedented extended, conformation. The NADH-binding domain consists of a five-stranded parallel, beta-sheet with four alpha-helices packing closely around this sheet., MMOR-FAD is structurally homologous to other FAD-containing, oxidoreductases, and we expect similar structures for the FAD/NADH-binding, domains of reductases that occur in other multicomponent monooxygenases.
About this StructureAbout this Structure
1TVC is a Single protein structure of sequence from Methylococcus capsulatus with FDA as ligand. Active as Methane monooxygenase, with EC number 1.14.13.25 Full crystallographic information is available from OCA.
ReferenceReference
NMR structure of the flavin domain from soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath)., Chatwood LL, Muller J, Gross JD, Wagner G, Lippard SJ, Biochemistry. 2004 Sep 28;43(38):11983-91. PMID:15379538
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