5GUP

Cryo-EM structure of mammalian respiratory supercomplex I1III2IV1

This is a non-PDB format compatible entry.

Summary for 5GUP

• Entry DOI: 10.2210/pdb5gup/pdb
• EMDB information: 9539
• Descriptor: Cytochrome c oxidase subunit 6C, NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12, ... (81 entities in total)
• Functional Keywords: cryo-em, mammalian, respiratory, supercomplex, electron transport
• Biological source: Sus scrofa (Pig); More
• Total number of polymer chains: 80
• Total formula weight: 1818749.11

Authors

Gu, J.,Wu, M.,Guo, R.,Yang, M. (deposition date: 2016-08-30, release date: 2017-03-29, Last modification date: 2019-11-06)

Primary citation

Wu, M.,Gu, J.,Guo, R.,Huang, Y.,Yang, M.
Structure of Mammalian Respiratory Supercomplex I1III2IV1
Cell, 167:1598-1609.e10, 2016

PubMed Abstract: The mammalian respiratory chain complexes assemble into supercomplexes (SCs) and reside in the inner mitochondrial membrane to transfer electrons and establish the proton gradient for complex V to synthesize ATP. The precise arrangement of SCs is largely unknown. Here, we report a 4.0-Å cryo-electron microscopy (cryo-EM) structure of the major SC in porcine heart, the 1.7-MDa SCIIIIIV. The complex III (CIII) dimer and complex IV (CIV) bind at the same side of the L-shaped complex I (CI). Several accessory or supernumerary subunits of CI, such as NDUFA11, NDUFB4, NDUFB8, and NDUFB9, directly contribute to the oligomerization of CI, CIII, and CIV. COX7C and COX7A of CIV attach CIV to the concave surface formed by CIII and the distal end of membrane arm of CI. The structure suggests a possible mechanism by which electrons are transferred from NADH to cytochrome c and provides a platform for future functional dissection of respiration.

PubMed: 27912063
DOI: 10.1016/j.cell.2016.11.012

Experimental method

ELECTRON MICROSCOPY (4 Å)