5xth

Cryo-EM structure of human respiratory supercomplex I1III2IV1

Loading... Status: waiting for Mol* initialization Structural highlights 5xth is a 16 chain structure with sequence from Bos taurus and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.9Å Ligands: 8Q1, CDL, CU, FES, FMN, HEA, HEC, HEM, MG, NDP, PEE, PLX, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CX6A2_BOVIN This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. Publication Abstract from PubMed 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-I2III2IV2 (MCI2III2IV2) with 140 subunits and a subset of associated cofactors using cryo-electron microscopy. The MCI2III2IV2 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 c1 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. Architecture of Human Mitochondrial Respiratory Megacomplex I2III2IV2.,Guo R, Zong S, Wu M, Gu J, Yang M Cell. 2017 Sep 7;170(6):1247-1257.e12. doi: 10.1016/j.cell.2017.07.050. Epub 2017, Aug 24. PMID:28844695 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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