9F5Z
Structure of the Chlamydomonas reinhardtii respiratory complex III from respiratory supercomplex
This is a non-PDB format compatible entry.
Summary for 9F5Z
| Entry DOI | 10.2210/pdb9f5z/pdb |
| EMDB information | 50204 |
| Descriptor | Cytochrome b, Cytochrome b-c1 complex subunit 7, 2,3-DIMETHOXY-5-METHYL-6-(3,11,15,19-TETRAMETHYL-EICOSA-2,6,10,14,18-PENTAENYL)-[1,4]BENZOQUINONE, ... (18 entities in total) |
| Functional Keywords | mitochondria, respiratory complex, respiration, alga, membrane protein |
| Biological source | Chlamydomonas reinhardtii More |
| Total number of polymer chains | 20 |
| Total formula weight | 533136.05 |
| Authors | Waltz, F.,Righetto, R.,Kotecha, A.,Engel, B.D. (deposition date: 2024-04-30, release date: 2025-03-12, Last modification date: 2025-04-02) |
| Primary citation | Waltz, F.,Righetto, R.D.,Lamm, L.,Salinas-Giege, T.,Kelley, R.,Zhang, X.,Obr, M.,Khavnekar, S.,Kotecha, A.,Engel, B.D. In-cell architecture of the mitochondrial respiratory chain. Science, 387:1296-1301, 2025 Cited by PubMed Abstract: Mitochondria regenerate adenosine triphosphate (ATP) through oxidative phosphorylation. This process is carried out by five membrane-bound complexes collectively known as the respiratory chain, working in concert to transfer electrons and pump protons. The precise organization of these complexes in native cells is debated. We used in situ cryo-electron tomography to visualize the native structures and organization of several major mitochondrial complexes in cells. ATP synthases and respiratory complexes segregate into curved and flat crista membrane domains, respectively. Respiratory complexes I, III, and IV assemble into a respirasome supercomplex, from which we determined a native 5-angstrom (Å) resolution structure showing binding of electron carrier cytochrome . Combined with single-particle cryo-electron microscopy at 2.4-Å resolution, we model how the respiratory complexes organize inside native mitochondria. PubMed: 40112058DOI: 10.1126/science.ads8738 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.39 Å) |
Structure validation
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