5NDC

Structure of ba3-type cytochrome c oxidase from Thermus thermophilus by serial femtosecond crystallography

5NDC の概要

• エントリーDOI: 10.2210/pdb5ndc/pdb
• 分子名称: Cytochrome c oxidase subunit 1, Cytochrome c oxidase subunit 2, Cytochrome c oxidase polypeptide IIA, ... (9 entities in total)
• 機能のキーワード: cytochrome c oxidase, oxidoreductase, sfx, respiratory chain enzyme
• 由来する生物種: Thermus thermophilus; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 92967.22

構造登録者

Andersson, R.,Safari, C.,Dods, R.,Nango, E.,Tanaka, R.,Nakane, T.,Tono, K.,Joti, Y.,Bath, P.,Dunevall, E.,Bosman, E.,Nureki, O.,Iwata, S.,Neutze, R.,Branden, G. (登録日: 2017-03-08, 公開日: 2017-08-23, 最終更新日: 2024-01-17)

主引用文献

Andersson, R.,Safari, C.,Dods, R.,Nango, E.,Tanaka, R.,Yamashita, A.,Nakane, T.,Tono, K.,Joti, Y.,Bath, P.,Dunevall, E.,Bosman, R.,Nureki, O.,Iwata, S.,Neutze, R.,Branden, G.
Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature.
Sci Rep, 7:4518-4518, 2017

PubMed Abstract: Cytochrome c oxidase catalyses the reduction of molecular oxygen to water while the energy released in this process is used to pump protons across a biological membrane. Although an extremely well-studied biological system, the molecular mechanism of proton pumping by cytochrome c oxidase is still not understood. Here we report a method to produce large quantities of highly diffracting microcrystals of ba -type cytochrome c oxidase from Thermus thermophilus suitable for serial femtosecond crystallography. The room-temperature structure of cytochrome c oxidase is solved to 2.3 Å resolution from data collected at an X-ray Free Electron Laser. We find overall agreement with earlier X-ray structures solved from diffraction data collected at cryogenic temperature. Previous structures solved from synchrotron radiation data, however, have shown conflicting results regarding the identity of the active-site ligand. Our room-temperature structure, which is free from the effects of radiation damage, reveals that a single-oxygen species in the form of a water molecule or hydroxide ion is bound in the active site. Structural differences between the ba -type and aa -type cytochrome c oxidases around the proton-loading site are also described.

PubMed: 28674417
DOI: 10.1038/s41598-017-04817-z

実験手法

X-RAY DIFFRACTION (2.3 Å)