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[[Image:1tvc.png|left|200px]]


{{STRUCTURE_1tvc| PDB=1tvc | SCENE= }}
==FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)==
<StructureSection load='1tvc' size='340' side='right'caption='[[1tvc]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1tvc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tvc OCA], [https://pdbe.org/1tvc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tvc RCSB], [https://www.ebi.ac.uk/pdbsum/1tvc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tvc ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tv/1tvc_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tvc ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


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


{{ABSTRACT_PUBMED_15379538}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1tvc" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
[[1tvc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TVC OCA].
*[[Methane monooxygenase 3D structures|Methane monooxygenase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:015379538</ref><references group="xtra"/>
__TOC__
[[Category: Methane monooxygenase]]
</StructureSection>
[[Category: Large Structures]]
[[Category: Methylococcus capsulatus]]
[[Category: Methylococcus capsulatus]]
[[Category: Chatwood, L L.]]
[[Category: Chatwood LL]]
[[Category: Gross, J D.]]
[[Category: Gross JD]]
[[Category: Lippard, S J.]]
[[Category: Lippard SJ]]
[[Category: Mueller, J.]]
[[Category: Mueller J]]
[[Category: Wagner, G.]]
[[Category: Wagner G]]
[[Category: Fad-binding]]
[[Category: Nadh-binding]]
[[Category: Oxidoreductase]]
Retrieved from "https://proteopedia.org/1tvc"