5XAM

Crystal structure of SecDF in I form at 4 A resolution

5XAM の概要

• エントリーDOI: 10.2210/pdb5xam/pdb
• 関連するPDBエントリー: 3AQP 5XAN 5XAP
• 分子名称: Protein translocase subunit SecD (1 entity in total)
• 機能のキーワード: membrane protein, alfa helical, sec translocon
• 由来する生物種: Deinococcus radiodurans str. R1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 161306.06

構造登録者

Tsukazaki, T.,Tanaka, Y.,Furukwa, A. (登録日: 2017-03-14, 公開日: 2017-05-17, 最終更新日: 2023-11-22)

主引用文献

Furukawa, A.,Yoshikaie, K.,Mori, T.,Mori, H.,Morimoto, Y.V.,Sugano, Y.,Iwaki, S.,Minamino, T.,Sugita, Y.,Tanaka, Y.,Tsukazaki, T.
Tunnel Formation Inferred from the I-Form Structures of the Proton-Driven Protein Secretion Motor SecDF
Cell Rep, 19:895-901, 2017

PubMed Abstract: Protein secretion mediated by SecYEG translocon and SecA ATPase is enhanced by membrane-embedded SecDF by using proton motive force. A previous structural study of SecDF indicated that it comprises 12 transmembrane helices that can conduct protons and three periplasmic domains, which form at least two characterized transition states, termed the F and I forms. We report the structures of full-length SecDF in I form at 2.6- to 2.8-Å resolution. The structures revealed that SecDF in I form can generate a tunnel that penetrates the transmembrane region and functions as a proton pathway regulated by a conserved Asp residue of the transmembrane region. In one crystal structure, periplasmic cavity interacts with a molecule, potentially polyethylene glycol, which may mimic a substrate peptide. This study provides structural insights into the Sec protein translocation that allows future analyses to develop a more detailed working model for SecDF.

PubMed: 28467902
DOI: 10.1016/j.celrep.2017.04.030

実験手法

X-RAY DIFFRACTION (4 Å)