2024-03-29T00:14:27Z
https://nagoya.repo.nii.ac.jp/oai
oai:nagoya.repo.nii.ac.jp:00025022
2023-01-16T04:15:42Z
336:695:696
Structural and Functional Analysis of the C-Terminal Region of FliG, an Essential Motor Component of Vibrio Na+-Driven Flagella
Miyanoiri, Yohei
74583
Hijikata, Atsushi
74584
Nishino, Yuuki
74585
Gohara, Mizuki
74586
Onoue, Yasuhiro
74587
Kojima, Seiji
74588
Kojima, Chojiro
74589
Shirai, Tsuyoshi
74590
Kainosho, Masatsune
74591
Homma, Michio
74592
FliG
flagellar motor
NMR
rotor
The flagellar motor protein complex consists of rotor and stator proteins. Their interaction generates torque of flagellum, which rotates bidirectionally, clockwise (CW) and counterclockwise. FliG, one of the rotor proteins, consists of three domains: N-terminal (FliGN), middle (FliGM), and C-terminal (FliGC). We have identified point mutations in FliGC from Vibrio alginolyticus, which affect the flagellar motility. To understand the molecular mechanisms, we explored the structural and dynamic properties of FliGC from both wild-type and motility-defective mutants. From nuclear magnetic resonance analysis, changes in signal intensities and chemical shifts between wild-type and the CW-biased mutant FliGC are observed in the Cα1-6 domain. Molecular dynamics simulations indicated the conformational dynamics of FliGC at sub-microsecond timescale, but not in the CW-biased mutant. Accordingly, we infer that the dynamic properties of atomic interactions around helix α1 in the Cα1-6 domain of FliGC contribute to ensure the precise regulation of the motor switching.
journal article
Elsevier
2017-10-03
application/pdf
STRUCTURE
10
25
1540
1548.e3
http://doi.org/10.1016/j.str.2017.08.010
http://hdl.handle.net/2237/27244
0969-2126
https://nagoya.repo.nii.ac.jp/record/25022/files/Miyanoiri-MS1-Structure-rev8.pdf
eng
https://doi.org/10.1016/j.str.2017.08.010
© 2017. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/