9DM1
Mycobacterial supercomplex malate:quinone oxidoreductase assembly
Summary for 9DM1
| Entry DOI | 10.2210/pdb9dm1/pdb |
| EMDB information | 46995 |
| Descriptor | Cytochrome c oxidase subunit 1, Cytochrome bc1 complex cytochrome c subunit, LpqE protein, ... (24 entities in total) |
| Functional Keywords | electron transport chain, mycobacterial ciii2civ2 supercomplex, membrane protein |
| Biological source | Mycolicibacterium smegmatis MC2 155 More |
| Total number of polymer chains | 25 |
| Total formula weight | 773332.55 |
| Authors | Di Trani, J.M.,Rubinstein, J.L. (deposition date: 2024-09-11, release date: 2024-10-23, Last modification date: 2025-03-05) |
| Primary citation | Di Trani, J.M.,Yu, J.,Courbon, G.M.,Lobez Rodriguez, A.P.,Cheung, C.Y.,Liang, Y.,Coupland, C.E.,Bueler, S.A.,Cook, G.M.,Brzezinski, P.,Rubinstein, J.L. Cryo-EM of native membranes reveals an intimate connection between the Krebs cycle and aerobic respiration in mycobacteria. Proc.Natl.Acad.Sci.USA, 122:e2423761122-e2423761122, 2025 Cited by PubMed Abstract: To investigate the structure of the mycobacterial oxidative phosphorylation machinery, we prepared inverted membrane vesicles from , enriched for vesicles containing complexes of interest, and imaged the vesicles with electron cryomicroscopy. We show that this analysis allows determination of the structure of both mycobacterial ATP synthase and the supercomplex of respiratory complexes III and IV in their native membrane. The latter structure reveals that the enzyme malate:quinone oxidoreductase (Mqo) physically associates with the respiratory supercomplex, an interaction that is lost on extraction of the proteins from the lipid bilayer. Mqo catalyzes an essential reaction in the Krebs cycle, and in vivo survival of mycobacterial pathogens is compromised when its activity is absent. We show with high-speed spectroscopy that the Mqo:supercomplex interaction enables rapid electron transfer from malate to the supercomplex. Further, the respiratory supercomplex is necessary for malate-driven, but not NADH-driven, electron transport chain activity and oxygen consumption. Together, these findings indicate a connection between the Krebs cycle and aerobic respiration that directs electrons along a single branch of the mycobacterial electron transport chain. PubMed: 39969994DOI: 10.1073/pnas.2423761122 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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