5IR6

The structure of bd oxidase from Geobacillus thermodenitrificans

5IR6 の概要

• エントリーDOI: 10.2210/pdb5ir6/pdb
• 分子名称: Bd-type quinol oxidase subunit I, Bd-type quinol oxidase subunit II, Putative membrane protein, ... (5 entities in total)
• 機能のキーワード: bd oxidase, terminal oxidase, oxidoreductase
• 由来する生物種: Geobacillus stearothermophilus K1041; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 94810.33

構造登録者

Safarian, S.,Mueller, H.,Rajendran, C.,Preu, J.,Ovchinnikov, S.,Kusumoto, T.,Hirose, T.,Langer, J.,Sakamoto, J.,Michel, H. (登録日: 2016-03-12, 公開日: 2016-05-04, 最終更新日: 2024-05-08)

主引用文献

Safarian, S.,Rajendran, C.,Muller, H.,Preu, J.,Langer, J.D.,Ovchinnikov, S.,Hirose, T.,Kusumoto, T.,Sakamoto, J.,Michel, H.
Structure of a bd oxidase indicates similar mechanisms for membrane-integrated oxygen reductases.
Science, 352:583-586, 2016

PubMed Abstract: The cytochrome bd oxidases are terminal oxidases that are present in bacteria and archaea. They reduce molecular oxygen (dioxygen) to water, avoiding the production of reactive oxygen species. In addition to their contribution to the proton motive force, they mediate viability under oxygen-related stress conditions and confer tolerance to nitric oxide, thus contributing to the virulence of pathogenic bacteria. Here we present the atomic structure of the bd oxidase from Geobacillus thermodenitrificans, revealing a pseudosymmetrical subunit fold. The arrangement and order of the heme cofactors support the conclusions from spectroscopic measurements that the cleavage of the dioxygen bond may be mechanistically similar to that in the heme-copper-containing oxidases, even though the structures are completely different.

PubMed: 27126043
DOI: 10.1126/science.aaf2477

実験手法

X-RAY DIFFRACTION (3.8 Å)