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5XTI

Cryo-EM architecture of human respiratory chain megacomplex-I2III2IV2

This is a non-PDB format compatible entry.
Summary for 5XTI
Entry DOI10.2210/pdb5xti/pdb
EMDB information6776
DescriptorNADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial, NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial, NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial, ... (82 entities in total)
Functional Keywordshomo sapiens, oxidoreductase, respiratory, oxidoreductase-electron transport complex, oxidoreductase/electron transport
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains138
Total formula weight2828802.58
Authors
Gu, J.,Wu, M.,Yang, M. (deposition date: 2017-06-19, release date: 2017-09-13, Last modification date: 2019-11-20)
Primary citationGuo, R.,Zong, S.,Wu, M.,Gu, J.,Yang, M.
Architecture of Human Mitochondrial Respiratory Megacomplex I2III2IV2.
Cell, 170:1247-1257.e12, 2017
Cited by
PubMed Abstract: The respiratory megacomplex represents the highest-order assembly of respiratory chain complexes, and it allows mitochondria to respond to energy-requiring conditions. To understand its architecture, we examined the human respiratory chain megacomplex-IIIIIV (MCIIIIIV) with 140 subunits and a subset of associated cofactors using cryo-electron microscopy. The MCIIIIIV forms a circular structure with the dimeric CIII located in the center, where it is surrounded by two copies each of CI and CIV. Two cytochrome c (Cyt.c) molecules are positioned to accept electrons on the surface of the c state CIII dimer. Analyses indicate that CII could insert into the gaps between CI and CIV to form a closed ring, which we termed the electron transport chain supercomplex. The structure not only reveals the precise assignment of individual subunits of human CI and CIII, but also enables future in-depth analysis of the electron transport chain as a whole.
PubMed: 28844695
DOI: 10.1016/j.cell.2017.07.050
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (17.4 Å)
Structure validation

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