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dc.contributor.authorPandini, A-
dc.contributor.authorMorcos, F-
dc.contributor.authorKhan, S-
dc.identifier.citationStructure, 24(7): 1209–1220, (2016)en_US
dc.description.abstractSwitching 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.en_US
dc.description.sponsorshipThe Royal Society Collaborative Exchange Grant Ul175.70592, the Molecular Biology Consortium (S.K) and the Francis Crick Institute which receives core funding from Cancer Research UK, the UK Medical Research Council, and Wellcome Trust through the Taylor (10179) group.en_US
dc.subjectFlagellar motor rotationen_US
dc.subjectBacterial chemotaxisen_US
dc.titleThe Gearbox of the bacterial flagellar motor switchen_US
Appears in Collections:Dept of Computer Science Research Papers

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