6F0K

Alternative complex III

6F0K の概要

• エントリーDOI: 10.2210/pdb6f0k/pdb
• EMDBエントリー: 4165
• 分子名称: Cytochrome c family protein, IRON/SULFUR CLUSTER, Fe-S-cluster-containing hydrogenase, ... (10 entities in total)
• 機能のキーワード: electron transfer, quinol oxidation, respiratory chain, membrane protein
• 由来する生物種: Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus obamensis); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 315835.21

構造登録者

Sousa, J.S.,Calisto, F.,Mills, D.J.,Pereira, M.M.,Vonck, J.,Kuehlbrandt, W. (登録日: 2017-11-20, 公開日: 2018-05-09, 最終更新日: 2025-07-02)

主引用文献

Sousa, J.S.,Calisto, F.,Langer, J.D.,Mills, D.J.,Refojo, P.N.,Teixeira, M.,Kuhlbrandt, W.,Vonck, J.,Pereira, M.M.
Structural basis for energy transduction by respiratory alternative complex III.
Nat Commun, 9:1728-1728, 2018

PubMed Abstract: Electron transfer in respiratory chains generates the electrochemical potential that serves as energy source for the cell. Prokaryotes can use a wide range of electron donors and acceptors and may have alternative complexes performing the same catalytic reactions as the mitochondrial complexes. This is the case for the alternative complex III (ACIII), a quinol:cytochrome c/HiPIP oxidoreductase. In order to understand the catalytic mechanism of this respiratory enzyme, we determined the structure of ACIII from Rhodothermus marinus at 3.9 Å resolution by single-particle cryo-electron microscopy. ACIII presents a so-far unique structure, for which we establish the arrangement of the cofactors (four iron-sulfur clusters and six c-type hemes) and propose the location of the quinol-binding site and the presence of two putative proton pathways in the membrane. Altogether, this structure provides insights into a mechanism for energy transduction and introduces ACIII as a redox-driven proton pump.

PubMed: 29712914
DOI: 10.1038/s41467-018-04141-8

実験手法

ELECTRON MICROSCOPY (3.87 Å)