5XTI
Cryo-EM architecture of human respiratory chain megacomplex-I2III2IV2
This is a non-PDB format compatible entry.
Summary for 5XTI
Entry DOI | 10.2210/pdb5xti/pdb |
EMDB information | 6776 |
Descriptor | NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial, NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial, NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial, ... (82 entities in total) |
Functional Keywords | homo sapiens, oxidoreductase, respiratory, oxidoreductase-electron transport complex, oxidoreductase/electron transport |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 138 |
Total formula weight | 2828802.58 |
Authors | |
Primary citation | Guo, 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: 28844695DOI: 10.1016/j.cell.2017.07.050 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (17.4 Å) |
Structure validation
Download full validation report