EMD-6716

Single-particle
25.0 Å
EMD-6716 Deposition: 16/03/2017
Map released: 12/04/2017
Last modified: 12/04/2017
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-6716

Ring assembly of FliF-FliG fusion protein

EMD-6716

Single-particle
25.0 Å
EMD-6716 Deposition: 16/03/2017
Map released: 12/04/2017
Last modified: 12/04/2017
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Salmonella enterica subsp. enterica serovar Typhimurium
Sample: FliFG fusion ring

Deposition Authors: Suzuki H, Yonekura K, Namba K
Structure of the rotor of the bacterial flagellar motor revealed by electron cryomicroscopy and single-particle image analysis
Suzuki H, Yonekura K , Namba K
(2004) J. Mol. Biol. , 337 , 105 - 113
PUBMED: 15001355
DOI: doi:10.1016/j.jmb.2004.01.034
ISSN: 0022-2836
ASTM: JMOBAK
Abstract:
The FliF ring is the base for self-assembly of the bacterial flagellum and the FliF/FliG ring complex is the core of the rotor of the flagellar motor. We report the structures of these two ring complexes obtained by electron cryomicroscopy and single-particle image analysis at 22A and 25A resolution, respectively. Direct comparison of these structures with the flagellar basal body made by superimposing the density maps on the central section reveals many interesting features, such as how the mechanically stable connection between the ring and the rod is formed, how directly FliF domains are involved in the near axial density of the basal body forming the proximal end of the central channel for a potential gating mechanism, some indication of flexibility in the connection of FliF and FliG, and structural and functional similarities to the head-to-tail connectors of bacteriophages.