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Title: Tunnel Formation Inferred from the I -Form Structures of the Proton-Driven Protein Secretion Motor SecDF
Authors: Furukawa, Arata
Yoshikaie, Kunihito
Mori, Takaharu
Mori, Hiroyuki  kyouindb  KAKEN_id  orcid (unconfirmed)
Morimoto, Yusuke V.
Sugano, Yasunori
Iwaki, Shigehiro
Minamino, Tohru
Sugita, Yuji
Tanaka, Yoshiki
Tsukazaki, Tomoya
Author's alias: 森, 博幸
Keywords: protein translocation
Sec proteins
membrane protein
crystal structure
Issue Date: 2-May-2017
Publisher: Elsevier BV
Journal title: Cell Reports
Volume: 19
Issue: 5
Start page: 895
End page: 901
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.
Rights: © 2017 The Authors. This article is under a Creative Commons license.
DOI(Published Version): 10.1016/j.celrep.2017.04.030
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