This entry represents the head subdomain from P1 domain from SecDF proteins, which constitutes a critical element for proton transport [1-3]. P1 domain P1 binds an unfolded protein, and undergoes functionally important conformational changes. SecDF functions as a membrane-integrated chaperone that mediates ATP-independent protein translocation. Paper describing PDB structure 3aqo. [1]. 21562494. Structure and function of a membrane component SecDF that enhances protein export. Tsukazaki T, Mori H, Echizen Y, Ishitani R, Fukai S, Tanaka T, Perederina A, Vassylyev DG, Kohno T, Maturana AD, Ito K, Nureki O;. Nature. 2011;474:235-238. Paper describing PDB structure 5mg3. [2]. 27924919. A central cavity within the holo-translocon suggests a mechanism for membrane protein insertion. Botte M, Zaccai NR, Nijeholt JL, Martin R, Knoops K, Papai G, Zou J, Deniaud A, Karuppasamy M, Jiang Q, Roy AS, Schulten K, Schultz P, Rappsilber J, Zaccai G, Berger I, Collinson I, Schaffitzel C;. Sci Rep. 2016;6:38399. Paper describing PDB structure 5xam. [3]. 28467902. Tunnel Formation Inferred from the I-Form Structures of the Proton-Driven Protein Secretion Motor SecDF. Furukawa A, Yoshikaie K, Mori T, Mori H, Morimoto YV, Sugano Y, Iwaki S, Minamino T, Sugita Y, Tanaka Y, Tsukazaki T;. Cell Rep. 2017;19:895-901. (from Pfam)
- Date:
- 2024-10-21