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8IB6

Respiratory complex Membrane domain of CI, focus-refined of type IA, Wild type mouse under cold temperature

Summary for 8IB6
Entry DOI10.2210/pdb8ib6/pdb
EMDB information35333
DescriptorNADH 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 Keywordsrespiratory complex, respiratory supercomplex, electron transport
Biological sourceMus musculus (house mouse)
More
Total number of polymer chains24
Total formula weight567536.53
Authors
Shin, Y.-C.,Liao, M. (deposition date: 2023-02-09, release date: 2024-09-18, Last modification date: 2024-11-20)
Primary citationShin, 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: 39395414
DOI: 10.1016/j.cell.2024.09.029
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

227561

건을2024-11-20부터공개중

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