1tvc

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[[Image:1tvc.gif|left|200px]]
 
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{{Structure
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==FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)==
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|PDB= 1tvc |SIZE=350|CAPTION= <scene name='initialview01'>1tvc</scene>
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<StructureSection load='1tvc' size='340' side='right'caption='[[1tvc]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FDA:DIHYDROFLAVINE-ADENINE+DINUCLEOTIDE'>FDA</scene>
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<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>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Methane_monooxygenase Methane monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.25 1.14.13.25] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= mmoC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=414 Methylococcus capsulatus])
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<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>
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|DOMAIN=
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<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>
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|RELATEDENTRY=[[1jq4|1JQ4]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tvc OCA], [http://www.ebi.ac.uk/pdbsum/1tvc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tvc RCSB]</span>
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== Function ==
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}}
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[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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tv/1tvc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1tvc" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Methane monooxygenase 3D structures|Methane monooxygenase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1TVC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TVC OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15379538 15379538]
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[[Category: Methane monooxygenase]]
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[[Category: Methylococcus capsulatus]]
[[Category: Methylococcus capsulatus]]
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[[Category: Single protein]]
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[[Category: Chatwood LL]]
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[[Category: Chatwood, L L.]]
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[[Category: Gross JD]]
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[[Category: Gross, J D.]]
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[[Category: Lippard SJ]]
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[[Category: Lippard, S J.]]
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[[Category: Mueller J]]
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[[Category: Mueller, J.]]
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[[Category: Wagner G]]
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[[Category: Wagner, G.]]
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[[Category: fad-binding]]
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[[Category: nadh-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:01:36 2008''
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Current revision

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

PDB ID 1tvc

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