3rfr

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<StructureSection load='3rfr' size='340' side='right'caption='[[3rfr]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
<StructureSection load='3rfr' size='340' side='right'caption='[[3rfr]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rfr]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylocystis_sp._m Methylocystis sp. m]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RFR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rfr]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylocystis_sp._M Methylocystis sp. M]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RFR FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CUA:DINUCLEAR+COPPER+ION'>CUA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.68&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1yew|1yew]], [[3chx|3chx]], [[3rgb|3rgb]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CUA:DINUCLEAR+COPPER+ION'>CUA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3rfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rfr OCA], [https://pdbe.org/3rfr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rfr RCSB], [https://www.ebi.ac.uk/pdbsum/3rfr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rfr 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=3rfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rfr OCA], [https://pdbe.org/3rfr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rfr RCSB], [https://www.ebi.ac.uk/pdbsum/3rfr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rfr ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9KX36_9HYPH Q9KX36_9HYPH]
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Particulate methane monooxygenase (pMMO) is an integral membrane metalloenzyme that oxidizes methane to methanol in methanotrophic bacteria. Previous biochemical and structural studies of pMMO have focused on preparations from Methylococcus capsulatus (Bath) and Methylosinus trichosporium OB3b. A pMMO from a third organism, Methylocystis species strain M, has been isolated and characterized. Both membrane-bound and solubilized Methylocystis sp. strain M pMMO contain approximately 2 copper ions per 100 kDa protomer and exhibit copper-dependent propylene epoxidation activity. Spectroscopic data indicate that Methylocystis sp. strain M pMMO contains a mixture of Cu(I) and Cu(II), of which the latter exhibits two distinct type 2 Cu(II) electron paramagnetic resonance (EPR) signals. Extended X-ray absorption fine structure (EXAFS) data are best fit with a mixture of Cu-O/N and Cu-Cu ligand environments with a Cu-Cu interaction at 2.52-2.64 A. The crystal structure of Methylocystis sp. strain M pMMO was determined to 2.68 A resolution and is the best quality pMMO structure obtained to date. It provides a revised model for the pmoA and pmoC subunits and has led to an improved model of M. capsulatus (Bath) pMMO. In these new structures, the intramembrane zinc/copper binding site has a different coordination environment from that in previous models.
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Crystal Structure and Characterization of Particulate Methane Monooxygenase from Methylocystis species Strain M.,Smith SM, Rawat S, Telser J, Hoffman BM, Stemmler TL, Rosenzweig AC Biochemistry. 2011 Nov 29;50(47):10231-40. Epub 2011 Nov 3. PMID:22013879<ref>PMID:22013879</ref>
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==See Also==
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*[[Methane monooxygenase 3D structures|Methane monooxygenase 3D structures]]
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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 3rfr" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Methylocystis sp. m]]
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[[Category: Methylocystis sp. M]]
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[[Category: Rosenzweig, A C]]
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[[Category: Rosenzweig AC]]
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[[Category: Smith, S M]]
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[[Category: Smith SM]]
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[[Category: Membrane]]
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[[Category: Oxidoreductase]]
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Current revision

Crystal Structure of particulate methane monooxygenase (pMMO) from Methylocystis sp. strain M

PDB ID 3rfr

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