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| | ==[2Fe-2S] Domain of Methane Monooxygenase Reductase from Methylococcus capsulatus (Bath)== | | ==[2Fe-2S] Domain of Methane Monooxygenase Reductase from Methylococcus capsulatus (Bath)== |
| - | <StructureSection load='1jq4' size='340' side='right'caption='[[1jq4]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='1jq4' size='340' side='right'caption='[[1jq4]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1jq4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Metca Metca]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JQ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JQ4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1jq4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylococcus_capsulatus_str._Bath Methylococcus capsulatus str. Bath]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JQ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JQ4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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='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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=1jq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jq4 OCA], [https://pdbe.org/1jq4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jq4 RCSB], [https://www.ebi.ac.uk/pdbsum/1jq4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jq4 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=1jq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jq4 OCA], [https://pdbe.org/1jq4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jq4 RCSB], [https://www.ebi.ac.uk/pdbsum/1jq4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jq4 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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| | ==See Also== | | ==See Also== |
| - | *[[Methane monooxygenase|Methane monooxygenase]] | + | *[[Methane monooxygenase 3D structures|Methane monooxygenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Metca]] | + | [[Category: Methylococcus capsulatus str. Bath]] |
| - | [[Category: Lippard, S J]] | + | [[Category: Lippard SJ]] |
| - | [[Category: Lugovskoy, A A]] | + | [[Category: Lugovskoy AA]] |
| - | [[Category: Mueller, J]] | + | [[Category: Mueller J]] |
| - | [[Category: Wagner, G]] | + | [[Category: Wagner G]] |
| - | [[Category: Oxidoreductase]]
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| Structural highlights
Function
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
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath) is a multicomponent enzyme system required for the conversion of methane to methanol. It comprises a hydroxylase, a regulatory protein, and a reductase. The reductase contains two domains: an NADH-binding and FAD-containing flavin domain and a ferredoxin (Fd) domain carrying a [2Fe-2S] cofactor. Here, we report the solution structure of the reduced form of the 98-amino acid Fd domain (Blazyk, J. L., and Lippard, S. J. Unpublished results) determined by nuclear magnetic resonance (NMR) spectroscopy and restrained molecular dynamics calculations. The structure consists of six beta strands arranged into two beta sheets as well as three alpha helices. Two of these helices form a helix-proline-helix motif, unprecedented among [2Fe-2S] proteins. The [2Fe-2S] cluster is coordinated by the sulfur atoms of cysteine residues 42, 47, 50, and 82. The 10.9 kDa ferredoxin domain of the reductase protein transfers electrons to carboxylate-bridged diiron centers in the 251 kDa hydroxylase component of sMMO. The binding of the Fd domain with the hydroxylase was investigated by NMR spectroscopy. The hydroxylase binding surface on the ferredoxin protein has a polar center surrounded by patches of hydrophobic residues. This arrangement of amino acids differs from that by which previously studied [2Fe-2S] proteins interact with their electron-transfer partners. The critical residues on the Fd domain involved in this binding interaction map well onto the universally conserved residues of sMMO enzymes from different species. We propose that the [2Fe-2S] domains in these other sMMO systems have a fold very similar to the one found here for M. capsulatus (Bath) MMOR-Fd.
NMR structure of the [2Fe-2S] ferredoxin domain from soluble methane monooxygenase reductase and interaction with its hydroxylase.,Muller J, Lugovskoy AA, Wagner G, Lippard SJ Biochemistry. 2002 Jan 8;41(1):42-51. PMID:11772001[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Muller J, Lugovskoy AA, Wagner G, Lippard SJ. NMR structure of the [2Fe-2S] ferredoxin domain from soluble methane monooxygenase reductase and interaction with its hydroxylase. Biochemistry. 2002 Jan 8;41(1):42-51. PMID:11772001
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