|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of particulate methane monooxygenase from Methylococcus capsulatus (Bath)== | | ==Crystal structure of particulate methane monooxygenase from Methylococcus capsulatus (Bath)== |
| - | <StructureSection load='3rgb' size='340' side='right' caption='[[3rgb]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='3rgb' size='340' side='right'caption='[[3rgb]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3rgb]] is a 9 chain structure with 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=3RGB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RGB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3rgb]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RGB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RGB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3chx|3chx]], [[3rfr|3rfr]], [[1yew|1yew]]</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> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methane_monooxygenase_(soluble) Methane monooxygenase (soluble)], with EC number [http://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=3rgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rgb OCA], [https://pdbe.org/3rgb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rgb RCSB], [https://www.ebi.ac.uk/pdbsum/3rgb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rgb ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rgb OCA], [http://pdbe.org/3rgb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rgb RCSB], [http://www.ebi.ac.uk/pdbsum/3rgb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rgb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/PMOB_METCA PMOB_METCA] |
| - | 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.
| + | |
| - | | + | |
| - | 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>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3rgb" 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: Large Structures]] |
| | [[Category: Methylococcus capsulatus]] | | [[Category: Methylococcus capsulatus]] |
| - | [[Category: Rosenzweig, A C]] | + | [[Category: Rosenzweig AC]] |
| - | [[Category: Smith, S M]] | + | [[Category: Smith SM]] |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
