1tvc

<StructureSection load='1tvc' size='340' side='right'caption='[[1tvc]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1tvc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acm_1292 Acm 1292]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TVC FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FDA:DIHYDROFLAVINE-ADENINE+DINUCLEOTIDE'>FDA</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jq4|1jq4]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mmoC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=414 ACM 1292])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methane_monooxygenase_(soluble) Methane monooxygenase (soluble)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.25 1.14.13.25] </span></td></tr>

[[https://www.uniprot.org/uniprot/MMOC_METCA MMOC_METCA]] Responsible for the initial oxygenation of methane to methanol in methanotrophs. It also catalyzes the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic and heterocyclic compounds. The component C is the iron-sulfur flavoprotein of sMMO.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:15379538</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1tvc" style="background-color:#fffaf0;"></div>

*[[Methane monooxygenase|Methane monooxygenase]]

[[Category: Acm 1292]]

[[Category: Chatwood, L L]]

[[Category: Gross, J D]]

[[Category: Lippard, S J]]

[[Category: Mueller, J]]

[[Category: Wagner, G]]

[[Category: Oxidoreductase]]