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-Structure paper
タイトル | Product analog binding identifies the copper active site of particulate methane monooxygenase. |
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ジャーナル・号・ページ | Nat Catal, Vol. 6, Issue 12, Page 1194-1204, Year 2023 |
掲載日 | 2023年11月6日 |
![]() | Frank J Tucci / Richard J Jodts / Brian M Hoffman / Amy C Rosenzweig / ![]() |
PubMed 要旨 | Nature's primary methane-oxidizing enzyme, the membrane-bound particulate methane monooxygenase (pMMO), catalyzes the oxidation of methane to methanol. pMMO activity requires copper, and decades of ...Nature's primary methane-oxidizing enzyme, the membrane-bound particulate methane monooxygenase (pMMO), catalyzes the oxidation of methane to methanol. pMMO activity requires copper, and decades of structural and spectroscopic studies have sought to identify the active site among three candidates: the Cu, Cu, and Cu sites. Challenges associated with the isolation of active pMMO have hindered progress toward locating its catalytic center. However, reconstituting pMMO into native lipid nanodiscs stabilizes its structure and recovers its activity. Here, these active samples were incubated with 2,2,2,-trifluoroethanol (TFE), a product analog that serves as a readily visualized active-site probe. Interactions of TFE with the Cu site were observed by both pulsed ENDOR spectroscopy and cryoEM, implicating Cu and the surrounding hydrophobic pocket as the likely site of methane oxidation. Use of these orthogonal techniques on parallel samples is a powerful approach that can circumvent difficulties in interpreting metalloenzyme cryoEM maps. |
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手法 | EM (単粒子) |
解像度 | 2.16 - 3.22 Å |
構造データ | EMDB-17287, PDB-8oyi: EMDB-40714, PDB-8sqw: EMDB-40717, PDB-8sr1: EMDB-40719, PDB-8sr4: EMDB-40720, PDB-8sr5: |
化合物 | ![]() ChemComp-CU: ![]() ChemComp-D10: ![]() ChemComp-PLC: ![]() ChemComp-P1O: ![]() ChemComp-HXG: ![]() ChemComp-ETF: ![]() ChemComp-HOH: ![]() ChemComp-WIY: |
由来 |
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![]() | OXIDOREDUCTASE / Metalloenzyme / Membrane Protein / Inhibitor / Nanodisc / Nanodiscs / Active Site |