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==FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)==
==FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)==
<StructureSection load='1tvc' size='340' side='right'caption='[[1tvc]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='1tvc' size='340' side='right'caption='[[1tvc]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<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='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>
</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='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='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='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>
<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>
<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>
</table>
== Function ==
== 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.  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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].
</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="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.
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>
</div>
<div class="pdbe-citations 1tvc" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Methane monooxygenase|Methane monooxygenase]]
*[[Methane monooxygenase 3D structures|Methane monooxygenase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Acm 1292]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chatwood, L L]]
[[Category: Methylococcus capsulatus]]
[[Category: Gross, J D]]
[[Category: Chatwood LL]]
[[Category: Lippard, S J]]
[[Category: Gross JD]]
[[Category: Mueller, J]]
[[Category: Lippard SJ]]
[[Category: Wagner, G]]
[[Category: Mueller J]]
[[Category: Fad-binding]]
[[Category: Wagner G]]
[[Category: Nadh-binding]]
[[Category: Oxidoreductase]]
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