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Remote Coupled Drastic β-Barrel to β-Sheet Transition of the Protein Translocation Motor.
- Source :
-
Structure (London, England : 1993) [Structure] 2018 Mar 06; Vol. 26 (3), pp. 485-489.e2. Date of Electronic Publication: 2018 Feb 01. - Publication Year :
- 2018
-
Abstract
- The membrane protein SecDF, belonging to the RND superfamily, enhances protein translocation at the extracytoplasmic side using a proton gradient. Here, we report the crystal structure of SecDF in a form we named Super-membrane-facing (Super F) form, demonstrating a β-barrel architecture instead of the previously reported β-sheet structure. Through this structural insight and supporting results of an in vivo crosslinking experiment, we propose a remote coupling model in which a structural change of the transmembrane region drives a functional, extracytoplasmic conformational transition.<br /> (Copyright © 2018 Elsevier Ltd. All rights reserved.)
- Subjects :
- Bacterial Proteins metabolism
Cell Membrane metabolism
Crystallography, X-Ray
Membrane Proteins metabolism
Membrane Transport Proteins metabolism
Models, Molecular
Protein Binding
Protein Conformation, beta-Strand
Protein Transport
Bacterial Proteins chemistry
Membrane Proteins chemistry
Membrane Transport Proteins chemistry
Thermus thermophilus metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1878-4186
- Volume :
- 26
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Structure (London, England : 1993)
- Publication Type :
- Academic Journal
- Accession number :
- 29398525
- Full Text :
- https://doi.org/10.1016/j.str.2018.01.002