1. Academic Validation
  2. Structure of the intact 14-subunit human cytochrome c oxidase

Structure of the intact 14-subunit human cytochrome c oxidase

  • Cell Res. 2018 Oct;28(10):1026-1034. doi: 10.1038/s41422-018-0071-1.
Shuai Zong # 1 Meng Wu # 1 Jinke Gu # 1 Tianya Liu # 1 Runyu Guo 1 Maojun Yang 2 3
Affiliations

Affiliations

  • 1 Ministry of Education Key Laboratory of Protein Science, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
  • 2 Ministry of Education Key Laboratory of Protein Science, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China. maojunyang@tsinghua.edu.cn.
  • 3 School of Pharmacy, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, Hubei, 430030, China. maojunyang@tsinghua.edu.cn.
  • # Contributed equally.
Abstract

Respiration is one of the most basic features of living organisms, and the electron transport chain complexes are probably the most complicated protein system in mitochondria. Complex-IV is the terminal Enzyme of the electron transport chain, existing either as randomly scattered complexes or as a component of supercomplexes. NDUFA4 was previously assumed as a subunit of complex-I, but recent biochemical data suggested it may be a subunit of complex-IV. However, no structural evidence supporting this notion was available till now. Here we obtained the 3.3 Å resolution structure of complex-IV derived from the human supercomplex I1III2IV1 and assigned the NDUFA4 subunit into complex-IV. Intriguingly, NDUFA4 lies exactly at the dimeric interface observed in previously reported crystal structures of complex-IV homodimer which would preclude complex-IV dimerization. Combining previous structural and biochemical data shown by us and other groups, we propose that the intact complex-IV is a monomer containing 14 subunits.

Figures