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| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[3chx]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylosinus_trichosporium Methylosinus trichosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CHX FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3chx]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylosinus_trichosporium Methylosinus trichosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CHX FirstGlance]. <br> |
| - | </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></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]] 3.9Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pmoB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=426 Methylosinus trichosporium]), pmoA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=426 Methylosinus trichosporium]), pmoC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=426 Methylosinus trichosporium])</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=3chx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3chx OCA], [https://pdbe.org/3chx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3chx RCSB], [https://www.ebi.ac.uk/pdbsum/3chx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3chx 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=3chx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3chx OCA], [https://pdbe.org/3chx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3chx RCSB], [https://www.ebi.ac.uk/pdbsum/3chx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3chx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9KX50_METTR Q9KX50_METTR] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 3chx" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3chx" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Methane monooxygenase 3D structures|Methane monooxygenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Methylosinus trichosporium]] | | [[Category: Methylosinus trichosporium]] |
| - | [[Category: Hakemian, A S]] | + | [[Category: Hakemian AS]] |
| - | [[Category: Beta barrel]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Methane]]
| + | |
| Structural highlights
Function
Q9KX50_METTR
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
Particulate methane monooxygenase (pMMO) is a membrane-bound metalloenzyme that oxidizes methane to methanol in methanotrophic bacteria. The nature of the pMMO active site and the overall metal content are controversial, with spectroscopic and crystallographic data suggesting the presence of a mononuclear copper center, a dinuclear copper center, a trinuclear center, and a diiron center or combinations thereof. Most studies have focused on pMMO from Methylococcus capsulatus (Bath). pMMO from a second organism, Methylosinus trichosporium OB3b, has been purified and characterized by spectroscopic and crystallographic methods. Purified M. trichosporium OB3b pMMO contains approximately 2 copper ions per 100 kDa protomer. Electron paramagnetic resonance (EPR) spectroscopic parameters indicate that type 2 Cu(II) is present as two distinct species. Extended X-ray absorption fine structure (EXAFS) data are best fit with oxygen/nitrogen ligands and reveal a Cu-Cu interaction at 2.52 A. Correspondingly, X-ray crystallography of M. trichosporium OB3b pMMO shows a dinuclear copper center, similar to that observed previously in the crystal structure of M. capsulatus (Bath) pMMO. There are, however, significant differences between the pMMO structures from the two organisms. A mononuclear copper center present in M. capsulatus (Bath) pMMO is absent in M. trichosporium OB3b pMMO, whereas a metal center occupied by zinc in the M. capsulatus (Bath) pMMO structure is occupied by copper in M. trichosporium OB3b pMMO. These findings extend previous work on pMMO from M. capsulatus (Bath) and provide new insight into the functional importance of the different metal centers.
The metal centers of particulate methane monooxygenase from Methylosinus trichosporium OB3b.,Hakemian AS, Kondapalli KC, Telser J, Hoffman BM, Stemmler TL, Rosenzweig AC Biochemistry. 2008 Jul 1;47(26):6793-801. Epub 2008 Jun 10. PMID:18540635[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hakemian AS, Kondapalli KC, Telser J, Hoffman BM, Stemmler TL, Rosenzweig AC. The metal centers of particulate methane monooxygenase from Methylosinus trichosporium OB3b. Biochemistry. 2008 Jul 1;47(26):6793-801. Epub 2008 Jun 10. PMID:18540635 doi:10.1021/bi800598h
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