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==== | ==cryoEM structure of particulate methane monooxygenase associated with Cu(I)== | ||
<StructureSection load='7ev9' size='340' side='right'caption='[[7ev9]]' scene=''> | <StructureSection load='7ev9' size='340' side='right'caption='[[7ev9]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7ev9]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylococcus_capsulatus_str._Bath Methylococcus capsulatus str. Bath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EV9 FirstGlance]. <br> | ||
</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=7ev9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ev9 OCA], [https://pdbe.org/7ev9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ev9 RCSB], [https://www.ebi.ac.uk/pdbsum/7ev9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ev9 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.6Å</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></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=7ev9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ev9 OCA], [https://pdbe.org/7ev9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ev9 RCSB], [https://www.ebi.ac.uk/pdbsum/7ev9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ev9 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/PMOB_METCA PMOB_METCA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The particulate methane monooxygenase (pMMO) is the first enzyme in the C1 metabolic pathway in methanotrophic bacteria. As this enzyme converts methane into methanol efficiently near room temperature, it has become the paradigm for developing an understanding of this difficult C1 chemistry. pMMO is a membrane-bound protein with three subunits (PmoB, PmoA, and PmoC) and 12-14 coppers distributed among different sites. X-ray crystal structures that have revealed only three mononuclear coppers at three sites have neither disclosed the location of the active site nor the catalytic mechanism of the enzyme. Here we report a cyro-EM structure of holo-pMMO from Methylococcus capsulatus (Bath) at 2.5 A, and develop quantitative electrostatic-potential profiling to scrutinize the nonprotein densities for signatures of the copper cofactors. Our results confirm a mononuclear Cu(I) at the A site, resolve two Cu(I)s at the B site, and uncover additional Cu(I) clusters at the PmoA/PmoC interface within the membrane (D site) and in the water-exposed C-terminal subdomain of the PmoB (E clusters). These findings complete the minimal set of copper factors required for catalytic turnover of pMMO, offering a glimpse of the catalytic machinery for methane oxidation according to the chemical principles underlying the mechanism proposed earlier. | |||
Copper Centers in the Cryo-EM Structure of Particulate Methane Monooxygenase Reveal the Catalytic Machinery of Methane Oxidation.,Chang WH, Lin HH, Tsai IK, Huang SH, Chung SC, Tu IP, Yu SS, Chan SI J Am Chem Soc. 2021 Jul 7;143(26):9922-9932. doi: 10.1021/jacs.1c04082. Epub 2021 , Jun 25. PMID:34170126<ref>PMID:34170126</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7ev9" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Methane monooxygenase 3D structures|Methane monooxygenase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Methylococcus capsulatus str. Bath]] | ||
[[Category: Chan SI]] | |||
[[Category: Chang WH]] | |||
[[Category: Chung SC]] | |||
[[Category: Huang SH]] | |||
[[Category: Lin HH]] | |||
[[Category: Tsai IK]] | |||
[[Category: Tu IP]] | |||
[[Category: Yu SF]] | |||
Latest revision as of 08:44, 5 June 2024
cryoEM structure of particulate methane monooxygenase associated with Cu(I)cryoEM structure of particulate methane monooxygenase associated with Cu(I)
Structural highlights
FunctionPublication Abstract from PubMedThe particulate methane monooxygenase (pMMO) is the first enzyme in the C1 metabolic pathway in methanotrophic bacteria. As this enzyme converts methane into methanol efficiently near room temperature, it has become the paradigm for developing an understanding of this difficult C1 chemistry. pMMO is a membrane-bound protein with three subunits (PmoB, PmoA, and PmoC) and 12-14 coppers distributed among different sites. X-ray crystal structures that have revealed only three mononuclear coppers at three sites have neither disclosed the location of the active site nor the catalytic mechanism of the enzyme. Here we report a cyro-EM structure of holo-pMMO from Methylococcus capsulatus (Bath) at 2.5 A, and develop quantitative electrostatic-potential profiling to scrutinize the nonprotein densities for signatures of the copper cofactors. Our results confirm a mononuclear Cu(I) at the A site, resolve two Cu(I)s at the B site, and uncover additional Cu(I) clusters at the PmoA/PmoC interface within the membrane (D site) and in the water-exposed C-terminal subdomain of the PmoB (E clusters). These findings complete the minimal set of copper factors required for catalytic turnover of pMMO, offering a glimpse of the catalytic machinery for methane oxidation according to the chemical principles underlying the mechanism proposed earlier. Copper Centers in the Cryo-EM Structure of Particulate Methane Monooxygenase Reveal the Catalytic Machinery of Methane Oxidation.,Chang WH, Lin HH, Tsai IK, Huang SH, Chung SC, Tu IP, Yu SS, Chan SI J Am Chem Soc. 2021 Jul 7;143(26):9922-9932. doi: 10.1021/jacs.1c04082. Epub 2021 , Jun 25. PMID:34170126[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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