- EMDB-9909: Salmonella hook in curved state - unsymmetrized cryo-EM map -
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Open data
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Basic information
Entry
Database: EMDB / ID: EMD-9909
Title
Salmonella hook in curved state - unsymmetrized cryo-EM map
Map data
full map
Sample
Complex: Bacterial flagellar polyhook
Protein or peptide: Flagellar hook protein FlgE
Keywords
bacterial / hook / flexible joint / flagella / MOTOR PROTEIN
Function / homology
Function and homology information
bacterial-type flagellum basal body / bacterial-type flagellum-dependent swarming motility Similarity search - Function
Flagellar hook protein FlgE superfamily / Flagellar hook protein FlgE / Flagellar basal body protein FlaE D2 domain / Flagellar basal body rod protein, conserved site / Flagellar hook-basal body protein, FlgE/F/G / Flagellar hook-basal body protein, FlgE/F/G-like / Flagella basal body rod proteins signature. / Flagellar basal body rod protein, N-terminal / Flagella basal body rod protein / Flagellar basal-body/hook protein, C-terminal domain / Flagellar basal body rod FlgEFG protein C-terminal Similarity search - Domain/homology
Japan Agency for Medical Research and Development (AMED)
JP18am0101076
Japan
Japan Society for the Promotion of Science
17K17085
Japan
Japan Society for the Promotion of Science
19K10083
Japan
Japan Society for the Promotion of Science
17K07318
Japan
Citation
Journal: Nat Struct Mol Biol / Year: 2019 Title: Torque transmission mechanism of the curved bacterial flagellar hook revealed by cryo-EM. Authors: Satoshi Shibata / Hideyuki Matsunami / Shin-Ichi Aizawa / Matthias Wolf / Abstract: Bacterial locomotion by rotating flagella is achieved through the hook, which transmits torque from the motor to the filament. The hook is a tubular structure composed of a single type of protein, ...Bacterial locomotion by rotating flagella is achieved through the hook, which transmits torque from the motor to the filament. The hook is a tubular structure composed of a single type of protein, yet it adopts a curved shape. To perform its function, it must be simultaneously flexible and torsionally rigid. The molecular mechanism by which chemically identical subunits form such a dynamic structure is unknown. Here, we show the complete structure of the hook from Salmonella enterica in its supercoiled 'curved' state, at 2.9 Å resolution. Subunits in the curved hook are grouped into 11 distinctive conformations, each shared along 11 protofilaments. The domains of the elongated hook subunit behave as rigid bodies connected by two hinge regions. The reconstituted model demonstrates how identical subunits can dynamically change conformation by physical interactions while bending. These multiple subunit states contradict the two-state model, which is a key feature of flagellar polymorphism.
History
Deposition
May 19, 2019
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Header (metadata) release
Oct 2, 2019
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Map release
Oct 2, 2019
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Update
Mar 27, 2024
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Current status
Mar 27, 2024
Processing site: PDBj / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 289 K / Instrument: FEI VITROBOT MARK IV / Details: 3 second blot, 4.0uL.
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Electron microscopy
Microscope
FEI TITAN KRIOS
Temperature
Min: 77.0 K / Max: 100.0 K
Details
nanoprobe, parallel beam illumination
Image recording
Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: INTEGRATING / Digitization - Dimensions - Width: 4000 pixel / Digitization - Dimensions - Height: 4000 pixel / Number grids imaged: 1 / Number real images: 2655 / Average exposure time: 2.0 sec. / Average electron dose: 89.0 e/Å2 Details: frame alignment and dose weighting using motioncor2
Electron beam
Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
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