8IB6
Respiratory complex Membrane domain of CI, focus-refined of type IA, Wild type mouse under cold temperature
Summary for 8IB6
Entry DOI | 10.2210/pdb8ib6/pdb |
EMDB information | 35333 |
Descriptor | NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11, NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial, ... (28 entities in total) |
Functional Keywords | respiratory complex, respiratory supercomplex, electron transport |
Biological source | Mus musculus (house mouse) More |
Total number of polymer chains | 24 |
Total formula weight | 567536.53 |
Authors | Shin, Y.-C.,Liao, M. (deposition date: 2023-02-09, 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 (3.3 Å) |
Structure validation
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