7ev9

cryoEM structure of particulate methane monooxygenase associated with Cu(I)

spinqualitylabelsall models 7ev9, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7ev9 is a 9 chain structure with sequence from Methylococcus capsulatus str. Bath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.6Å Ligands: CU1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PMOB_METCA 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Methane monooxygenase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA