5IY5

Electron transfer complex of cytochrome c and cytochrome c oxidase at 2.0 angstrom resolution

Summary for 5IY5

• Entry DOI: 10.2210/pdb5iy5/pdb
• Related: 5B3S
• Descriptor: Cytochrome c oxidase subunit 1, Cytochrome c oxidase subunit 7A1, mitochondrial, Cytochrome c oxidase subunit 7B, mitochondrial, ... (32 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: Bos taurus (Bovine); More
• Total number of polymer chains: 28
• Total formula weight: 456564.57

Authors

Shimada, S.,Baba, J.,Aoe, S.,Shimada, A.,Yamashita, E.,Tsukihara, T. (deposition date: 2016-03-24, release date: 2017-01-11, Last modification date: 2023-11-08)

Primary citation

Shimada, S.,Shinzawa-Itoh, K.,Baba, J.,Aoe, S.,Shimada, A.,Yamashita, E.,Kang, J.,Tateno, M.,Yoshikawa, S.,Tsukihara, T.
Complex structure of cytochrome c-cytochrome c oxidase reveals a novel protein-protein interaction mode
EMBO J., 36:291-300, 2017

PubMed Abstract: Mitochondrial cytochrome c oxidase (CcO) transfers electrons from cytochrome c (Cyt.c) to O to generate HO, a process coupled to proton pumping. To elucidate the mechanism of electron transfer, we determined the structure of the mammalian Cyt.c-CcO complex at 2.0-Å resolution and identified an electron transfer pathway from Cyt.c to CcO. The specific interaction between Cyt.c and CcO is stabilized by a few electrostatic interactions between side chains within a small contact surface area. Between the two proteins are three water layers with a long inter-molecular span, one of which lies between the other two layers without significant direct interaction with either protein. Cyt.c undergoes large structural fluctuations, using the interacting regions with CcO as a fulcrum. These features of the protein-protein interaction at the docking interface represent the first known example of a new class of protein-protein interaction, which we term "soft and specific". This interaction is likely to contribute to the rapid association/dissociation of the Cyt.c-CcO complex, which facilitates the sequential supply of four electrons for the O reduction reaction.

PubMed: 27979921
DOI: 10.15252/embj.201695021

Experimental method

X-RAY DIFFRACTION (2 Å)