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| | <StructureSection load='6cpd' size='340' side='right'caption='[[6cpd]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='6cpd' size='340' side='right'caption='[[6cpd]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6cpd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Methylocystis_sp._atcc_49242 Methylocystis sp. atcc 49242]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CPD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CPD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6cpd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylocystis_sp._ATCC_49242 Methylocystis sp. ATCC 49242]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CPD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.903Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Met49242_1452 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=622637 Methylocystis sp. ATCC 49242])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6cpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpd OCA], [http://pdbe.org/6cpd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cpd RCSB], [http://www.ebi.ac.uk/pdbsum/6cpd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cpd 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=6cpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpd OCA], [https://pdbe.org/6cpd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cpd RCSB], [https://www.ebi.ac.uk/pdbsum/6cpd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cpd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A452CSS7_9HYPH A0A452CSS7_9HYPH] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Methylocystis sp. atcc 49242]] | + | [[Category: Methylocystis sp. ATCC 49242]] |
| - | [[Category: Fisher, O S]] | + | [[Category: Fisher OS]] |
| - | [[Category: Rosenzweig, A C]] | + | [[Category: Rosenzweig AC]] |
| - | [[Category: Copper]]
| + | |
| - | [[Category: Cupredoxin]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Periplasm]]
| + | |
| Structural highlights
Function
A0A452CSS7_9HYPH
Publication Abstract from PubMed
Methane-oxidizing microbes catalyze the oxidation of the greenhouse gas methane using the copper-dependent enzyme particulate methane monooxygenase (pMMO). Isolated pMMO exhibits lower activity than whole cells, however, suggesting that additional components may be required. A pMMO homolog, ammonia monooxygenase (AMO), converts ammonia to hydroxylamine in ammonia-oxidizing bacteria (AOB) which produce another potent greenhouse gas, nitrous oxide. Here we show that PmoD, a protein encoded within many pmo operons that is homologous to the AmoD proteins encoded within AOB amo operons, forms a copper center that exhibits the features of a well-defined CuA site using a previously unobserved ligand set derived from a cupredoxin homodimer. PmoD is critical for copper-dependent growth on methane, and genetic analyses strongly support a role directly related to pMMO and AMO. These findings identify a copper-binding protein that may represent a missing link in the function of enzymes critical to the global carbon and nitrogen cycles.
Characterization of a long overlooked copper protein from methane- and ammonia-oxidizing bacteria.,Fisher OS, Kenney GE, Ross MO, Ro SY, Lemma BE, Batelu S, Thomas PM, Sosnowski VC, DeHart CJ, Kelleher NL, Stemmler TL, Hoffman BM, Rosenzweig AC Nat Commun. 2018 Oct 15;9(1):4276. doi: 10.1038/s41467-018-06681-5. PMID:30323281[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fisher OS, Kenney GE, Ross MO, Ro SY, Lemma BE, Batelu S, Thomas PM, Sosnowski VC, DeHart CJ, Kelleher NL, Stemmler TL, Hoffman BM, Rosenzweig AC. Characterization of a long overlooked copper protein from methane- and ammonia-oxidizing bacteria. Nat Commun. 2018 Oct 15;9(1):4276. doi: 10.1038/s41467-018-06681-5. PMID:30323281 doi:http://dx.doi.org/10.1038/s41467-018-06681-5
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