Downloads: 102

Files in This Item:
File Description SizeFormat 
j.celrep.2017.04.030.pdf3.46 MBAdobe PDFView/Open
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 https://orcid.org/0000-0002-0429-1269 (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
SecYEG
SecDF
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.
URI: http://hdl.handle.net/2433/227558
DOI(Published Version): 10.1016/j.celrep.2017.04.030
Appears in Collections:Journal Articles

Show full item record

Export to RefWorks


Export Format: 


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.