Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Diverse high-torque bacterial flagellar motors assemble wider stator rings using a conserved protein scaffold.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 113, Issue 13, Page E1917-E1926, Year 2016
Publish date	Mar 29, 2016
Authors	Morgan Beeby / Deborah A Ribardo / Caitlin A Brennan / Edward G Ruby / Grant J Jensen / David R Hendrixson /
PubMed Abstract	Although it is known that diverse bacterial flagellar motors produce different torques, the mechanism underlying torque variation is unknown. To understand this difference better, we combined genetic ...Although it is known that diverse bacterial flagellar motors produce different torques, the mechanism underlying torque variation is unknown. To understand this difference better, we combined genetic analyses with electron cryo-tomography subtomogram averaging to determine in situ structures of flagellar motors that produce different torques, from Campylobacter and Vibrio species. For the first time, to our knowledge, our results unambiguously locate the torque-generating stator complexes and show that diverse high-torque motors use variants of an ancestrally related family of structures to scaffold incorporation of additional stator complexes at wider radii from the axial driveshaft than in the model enteric motor. We identify the protein components of these additional scaffold structures and elucidate their sequential assembly, demonstrating that they are required for stator-complex incorporation. These proteins are widespread, suggesting that different bacteria have tailored torques to specific environments by scaffolding alternative stator placement and number. Our results quantitatively account for different motor torques, complete the assignment of the locations of the major flagellar components, and provide crucial constraints for understanding mechanisms of torque generation and the evolution of multiprotein complexes.
External links	Proc Natl Acad Sci U S A / PubMed:26976588 / PubMed Central
Methods	EM (subtomogram averaging) / EM (tomography)
Resolution	44.0 - 85.3 Å
Structure data	EMDB-3150: Diverse high-torque bacterial flagellar motors assemble wider stator rings using a conserved protein scaffold Method: EM (subtomogram averaging) / Resolution: 44.0 Å EMDB-3154: Salmonella enterica wild-type bacterial flagellar motor Method: EM (subtomogram averaging) / Resolution: 69.4 Å EMDB-3155: Vibrio fischeri wild-type bacterial flagellar motor Method: EM (subtomogram averaging) / Resolution: 63.0 Å EMDB-3156: Vibrio fischeri motB deletion bacterial flagellar motor Method: EM (subtomogram averaging) / Resolution: 70.3 Å EMDB-3157: Campylobacter jejuni motB deletion bacterial flagellar motor Method: EM (subtomogram averaging) / Resolution: 45.8 Å EMDB-3158: Campylobacter jejuni flgQ deletion bacterial flagellar motor Method: EM (subtomogram averaging) / Resolution: 60.1 Å EMDB-3159: Campylobacter jejuni flgP deletion bacterial flagellar motor Method: EM (subtomogram averaging) / Resolution: 61.2 Å EMDB-3160: Campylobacter jejuni pflA deletion bacterial flagellar motor Method: EM (subtomogram averaging) / Resolution: 85.3 Å EMDB-3161: Campylobacter jejuni pflB deletion bacterial flagellar motor Method: EM (subtomogram averaging) / Resolution: 61.9 Å EMDB-3162: Vibrio fischeri flgP deletion bacterial flagellar motor Method: EM (subtomogram averaging) / Resolution: 81.0 Å EMDB-3813: Tomogram of the salmonella enterica wild-type bacterial flagellar motor Method: EM (tomography)
Source	Campylobacter jejuni (Campylobacter) Salmonella enterica (bacteria) Aliivibrio fischeri (bacteria) Salmonella (bacteria)