Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5J4Z

Architecture of tight respirasome

This is a non-PDB format compatible entry.
Summary for 5J4Z
Entry DOI10.2210/pdb5j4z/pdb
EMDB information8130
DescriptorCOMPLEX I ND3, COMPLEX I ND6, COMPLEX I ND4L, ... (80 entities in total)
Functional Keywordsmembrane protein complex, supercomplex, respirasome, electron transport
Biological sourceOvis aries (SHEEP)
More
Total number of polymer chains89
Total formula weight1285297.38
Authors
Letts, J.A.,Fiedorczuk, K.,Sazanov, L.A. (deposition date: 2016-04-01, release date: 2016-09-21, Last modification date: 2024-10-23)
Primary citationLetts, J.A.,Fiedorczuk, K.,Sazanov, L.A.
The architecture of respiratory supercomplexes.
Nature, 537:644-648, 2016
Cited by
PubMed Abstract: Mitochondrial electron transport chain complexes are organized into supercomplexes responsible for carrying out cellular respiration. Here we present three architectures of mammalian (ovine) supercomplexes determined by cryo-electron microscopy. We identify two distinct arrangements of supercomplex CICIIICIV (the respirasome)-a major 'tight' form and a minor 'loose' form (resolved at the resolution of 5.8 Å and 6.7 Å, respectively), which may represent different stages in supercomplex assembly or disassembly. We have also determined an architecture of supercomplex CICIII at 7.8 Å resolution. All observed density can be attributed to the known 80 subunits of the individual complexes, including 132 transmembrane helices. The individual complexes form tight interactions that vary between the architectures, with complex IV subunit COX7a switching contact from complex III to complex I. The arrangement of active sites within the supercomplex may help control reactive oxygen species production. To our knowledge, these are the first complete architectures of the dominant, physiologically relevant state of the electron transport chain.
PubMed: 27654913
DOI: 10.1038/nature19774
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (5.8 Å)
Structure validation

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon