8IBG
Respiratory complex CIII2, focus-refined of type II, Wild type mouse under cold temperature
This is a non-PDB format compatible entry.
Summary for 8IBG
| Entry DOI | 10.2210/pdb8ibg/pdb |
| EMDB information | 35343 |
| Descriptor | Cytochrome b-c1 complex subunit 1, mitochondrial, Cytochrome b-c1 complex subunit 10, PROTOPORPHYRIN IX CONTAINING FE, ... (17 entities in total) |
| Functional Keywords | respiratory complex, respiratory supercomplex, electron transport |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 22 |
| Total formula weight | 584541.71 |
| Authors | Shin, Y.-C.,Liao, M. (deposition date: 2023-02-10, release date: 2024-09-18, Last modification date: 2024-10-30) |
| Primary citation | Shin, Y.C.,Latorre-Muro, P.,Djurabekova, A.,Zdorevskyi, O.,Bennett, C.F.,Burger, N.,Song, K.,Xu, C.,Paulo, J.A.,Gygi, S.P.,Sharma, V.,Liao, M.,Puigserver, P. Structural basis of respiratory complex adaptation to cold temperatures. Cell, 2024 Cited by PubMed Abstract: In response to cold, mammals activate brown fat for respiratory-dependent thermogenesis reliant on the electron transport chain. Yet, the structural basis of respiratory complex adaptation upon cold exposure remains elusive. Herein, we combined thermoregulatory physiology and cryoelectron microscopy (cryo-EM) to study endogenous respiratory supercomplexes from mice exposed to different temperatures. A cold-induced conformation of CI:III (termed type 2) supercomplex was identified with a ∼25° rotation of CIII around its inter-dimer axis, shortening inter-complex Q exchange space, and exhibiting catalytic states that favor electron transfer. Large-scale supercomplex simulations in mitochondrial membranes reveal how lipid-protein arrangements stabilize type 2 complexes to enhance catalytic activity. Together, our cryo-EM studies, multiscale simulations, and biochemical analyses unveil the thermoregulatory mechanisms and dynamics of increased respiratory capacity in brown fat at the structural and energetic level. PubMed: 39395414DOI: 10.1016/j.cell.2024.09.029 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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