Transient protein interactions are paramount to life where fast and efficient transfer of information and cargo are often integral to pathways and networks. However, complexes formed by transient protein interactions are often times resistant to direct structural characterization due to their inherent, dynamic nature, so our knowledge to date typically derives from biochemical, biophysical and computational methods. In this issue, Shimada and co‐authors present the crystal structure of the mammalian cytochrome c oxidase in complex with its electron donor cytochrome c, identifying a new class of protein–protein interaction termed “soft and specific”.
See also: S Shimada et al (February 2017)
Cytochrome c oxidase (Complex IV, CcO) is a member of the haem copper oxidase superfamily (HCO), which functions as the terminal enzyme in the respiratory chain of mitochondria and aerobic prokaryotes (Ferguson‐Miller & Babcock, 1996). It couples the reduction in molecular oxygen to transmembrane proton pumping driving downstream adenosine triphosphate (ATP) biosynthesis. The mechanisms governing the electron and proton transfer reactions in the individual respiratory complexes have been areas of study for decades.
It has been over 20 years since Tsukihara et al reported …
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