1TVC

FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)

Summary for 1TVC

• Entry DOI: 10.2210/pdb1tvc/pdb
• Related: 1JQ4
• NMR Information: BMRB: 6295
• Descriptor: METHANE MONOOXYGENASE COMPONENT C, DIHYDROFLAVINE-ADENINE DINUCLEOTIDE (2 entities in total)
• Functional Keywords: fad-binding; nadh-binding, oxidoreductase
• Biological source: Methylococcus capsulatus
• Total number of polymer chains: 1
• Total formula weight: 28441.82

Authors

Chatwood, L.L.,Mueller, J.,Gross, J.D.,Wagner, G.,Lippard, S.J. (deposition date: 2004-06-29, release date: 2004-10-12, Last modification date: 2024-05-22)

Primary citation

Chatwood, L.L.,Gross, J.D.,Wagner, G.,Lippard, S.J.
NMR Structure of the Flavin Domain from Soluble Methane Monooxygenase Reductase from Methylococcus capsulatus (Bath)
Biochemistry, 43:11983-11991, 2004

PubMed Abstract: 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.

PubMed: 15379538
DOI: 10.1021/bi049066n

Experimental method

SOLUTION NMR