6U8Y
Structure of the membrane-bound sulfane sulfur reductase (MBS), an archaeal respiratory membrane complex
6U8Y の概要
| エントリーDOI | 10.2210/pdb6u8y/pdb |
| EMDBエントリー | 20692 |
| 分子名称 | Monovalent cation/H+ antiporter subunit E, NADH dehydrogenase subunit C, NADH dehydrogenase subunit D, ... (14 entities in total) |
| 機能のキーワード | cryoem, membrane protein, respiratory system |
| 由来する生物種 | Pyrococcus furiosus COM1 詳細 |
| タンパク質・核酸の鎖数 | 26 |
| 化学式量合計 | 717706.79 |
| 構造登録者 | |
| 主引用文献 | Yu, H.,Haja, D.K.,Schut, G.J.,Wu, C.H.,Meng, X.,Zhao, G.,Li, H.,Adams, M.W.W. Structure of the respiratory MBS complex reveals iron-sulfur cluster catalyzed sulfane sulfur reduction in ancient life. Nat Commun, 11:5953-5953, 2020 Cited by PubMed Abstract: Modern day aerobic respiration in mitochondria involving complex I converts redox energy into chemical energy and likely evolved from a simple anaerobic system now represented by hydrogen gas-evolving hydrogenase (MBH) where protons are the terminal electron acceptor. Here we present the cryo-EM structure of an early ancestor in the evolution of complex I, the elemental sulfur (S)-reducing reductase MBS. Three highly conserved protein loops linking cytoplasmic and membrane domains enable scalable energy conversion in all three complexes. MBS contains two proton pumps compared to one in MBH and likely conserves twice the energy. The structure also reveals evolutionary adaptations of MBH that enabled S reduction by MBS catalyzed by a site-differentiated iron-sulfur cluster without participation of protons or amino acid residues. This is the simplest mechanism proposed for reduction of inorganic or organic disulfides. It is of fundamental significance in the iron and sulfur-rich volcanic environments of early earth and possibly the origin of life. MBS provides a new perspective on the evolution of modern-day respiratory complexes and of catalysis by biological iron-sulfur clusters. PubMed: 33230146DOI: 10.1038/s41467-020-19697-7 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (4 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






