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Two-ball structure of the flagellar hook-length control protein FliK as revealed by high-speed atomic force microscopy.
- Source :
-
Journal of molecular biology [J Mol Biol] 2015 Jan 30; Vol. 427 (2), pp. 406-14. Date of Electronic Publication: 2014 Nov 15. - Publication Year :
- 2015
-
Abstract
- The bacterial flagellar hook is a short and uniquely curved tube that connects the basal body to the filament. Hook length is controlled at 55 nm on average by a soluble protein FliK in Salmonella enterica serovar Typhimurium. The N-terminal segment of FliK responsible for measuring the hook length is considered to be intrinsically disordered. Here, we show by high-speed atomic force microscopy that a FliK molecule in solution takes on a shape of two balls linked by a flexible string; the larger ball corresponds to the N-terminal region and the smaller one corresponds to the C-terminal region. The N-terminal domain is stable but the C-terminal domain fluctuates in shape. Based on these and other features of FliK, we propose that the folding of the N-terminal segment at the tip of the growing hook plays a major role in determining the minimal length of the hook.<br /> (Copyright © 2014. Published by Elsevier Ltd.)
Details
- Language :
- English
- ISSN :
- 1089-8638
- Volume :
- 427
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Journal of molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 25463436
- Full Text :
- https://doi.org/10.1016/j.jmb.2014.11.007