2N4X

Structure of the Transmembrane Electron Transporter CcdA

2N4X の概要

• エントリーDOI: 10.2210/pdb2n4x/pdb
• NMR情報: BMRB: 25685
• 分子名称: Cytochrome C-type biogenesis protein (CcdA) (1 entity in total)
• 機能のキーワード: transmembrane electron transporter, transmembrane reductase, ccda, dsbd homolog, membrane protein
• 由来する生物種: Archaeoglobus fulgidus DSM 4304
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22771.21

構造登録者

Chou, J.J.,Williamson, J.A. (登録日: 2015-07-01, 公開日: 2016-05-18, 最終更新日: 2024-05-15)

主引用文献

Williamson, J.A.,Cho, S.H.,Ye, J.,Collet, J.F.,Beckwith, J.R.,Chou, J.J.
Structure and multistate function of the transmembrane electron transporter CcdA.
Nat.Struct.Mol.Biol., 22:809-814, 2015

PubMed Abstract: The mechanism by which transmembrane reductases use a single pair of cysteine residues to relay electrons between protein substrates across biological membranes is a long-standing mystery in thiol-redox biochemistry. Here we show the NMR structure of a reduced-state mimic of archaeal CcdA, a protein that transfers electrons across the inner membrane, by using a redox-active NMR sample. The two cysteine positions in CcdA are separated by 20 Å. Whereas one is accessible to the cytoplasm, the other resides in the protein core, thus implying that conformational exchange is required for periplasmic accessibility. In vivo mixed disulfide-trapping experiments validated the functional positioning of the cysteines, and in vitro accessibility results confirmed conformational exchange. Our NMR and functional data together show the existence of multiple conformational states and suggest a four-state model for relaying electrons from cytosolic to periplasmic redox substrates.

PubMed: 26389738
DOI: 10.1038/nsmb.3099

実験手法

SOLUTION NMR