Please use this identifier to cite or link to this item: http://buratest.brunel.ac.uk/handle/2438/12944
Title: The Gearbox of the bacterial flagellar motor switch
Authors: Pandini, A
Morcos, F
Khan, S
Keywords: Flagellar motor rotation;Bacterial chemotaxis
Issue Date: 2016
Publisher: Elsevier
Citation: Structure, 24(7): 1209–1220, (2016)
Abstract: Switching of flagellar motor rotation sense dictates bacterial chemotaxis. Multi-subunit FliM-FliG rotor rings couple signal protein binding in FliM with reversal of a distant FliG C-terminal (FliGC) helix involved in stator contacts. Subunit dynamics were examined in conformer ensembles generated by molecular simulations from the X-ray structures. Principal component analysis extracted collective motions. Interfacial loop immobilization by complex formation coupled elastic fluctuations of the FliM middle (FliMM) and FliG middle (FliGM) domains. Coevolved mutations captured interfacial dynamics as well as contacts. FliGM rotation was amplified via two central hinges to the FliGC helix. Intrinsic flexibility, reported by the FliGMC ensembles, reconciled conformers with opposite FliGC helix orientations. FliG domain stacking deformed the inter-domain linker and reduced flexibility; but conformational changes were not triggered by engineered linker deletions that cause a rotation-locked phenotype. These facts suggest that binary rotation states arise from conformational selection by stacking interactions.
URI: http://www.sciencedirect.com/science/article/pii/S0969212616301186
http://bura.brunel.ac.uk/handle/2438/12944
DOI: http://dx.doi.org/10.1016/j.str.2016.05.012
ISSN: 0969-2126
Appears in Collections:Dept of Computer Science Research Papers

Files in This Item:
File Description SizeFormat 
Fulltext.pdf4.18 MBAdobe PDFView/Open


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