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Yorodumi- PDB-8upl: Cryo-EM structure of a Clockwise locked form of the Salmonella en... -
+Open data
-Basic information
Entry | Database: PDB / ID: 8upl | |||||||||||||||
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Title | Cryo-EM structure of a Clockwise locked form of the Salmonella enterica Typhimurium flagellar C-ring, with C34 symmetry applied | |||||||||||||||
Components |
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Keywords | MOTOR PROTEIN / Flagella / Salmonella / C-ring / motor | |||||||||||||||
Function / homology | Function and homology information bacterial-type flagellum basal body, MS ring / bacterial-type flagellum basal body / bacterial-type flagellum-dependent swarming motility / positive chemotaxis / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / chemotaxis / plasma membrane Similarity search - Function | |||||||||||||||
Biological species | Salmonella enterica subsp. enterica serovar Typhimurium (bacteria) | |||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 5.4 Å | |||||||||||||||
Authors | Johnson, S. / Deme, J.C. / Lea, S.M. | |||||||||||||||
Funding support | United States, United Kingdom, 4items
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Citation | Journal: Nat Microbiol / Year: 2024 Title: Structural basis of directional switching by the bacterial flagellum. Authors: Steven Johnson / Justin C Deme / Emily J Furlong / Joseph J E Caesar / Fabienne F V Chevance / Kelly T Hughes / Susan M Lea / Abstract: The bacterial flagellum is a macromolecular protein complex that harvests energy from uni-directional ion flow across the inner membrane to power bacterial swimming via rotation of the flagellar ...The bacterial flagellum is a macromolecular protein complex that harvests energy from uni-directional ion flow across the inner membrane to power bacterial swimming via rotation of the flagellar filament. Rotation is bi-directional, with binding of a cytoplasmic chemotactic response regulator controlling reversal, though the structural and mechanistic bases for rotational switching are not well understood. Here we present cryoelectron microscopy structures of intact Salmonella flagellar basal bodies (3.2-5.5 Å), including the cytoplasmic C-ring complexes required for power transmission, in both counter-clockwise and clockwise rotational conformations. These reveal 180° movements of both the N- and C-terminal domains of the FliG protein, which, when combined with a high-resolution cryoelectron microscopy structure of the MotAB stator, show that the stator shifts from the outside to the inside of the C-ring. This enables rotational switching and reveals how uni-directional ion flow across the inner membrane is used to accomplish bi-directional rotation of the flagellum. | |||||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8upl.cif.gz | 6.4 MB | Display | PDBx/mmCIF format |
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PDB format | pdb8upl.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 8upl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/up/8upl ftp://data.pdbj.org/pub/pdb/validation_reports/up/8upl | HTTPS FTP |
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-Related structure data
Related structure data | 42451MC 8ucsC 8umdC 8umxC 8uoxC C: citing same article (ref.) M: map data used to model this data |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 61295.645 Da / Num. of mol.: 34 / Source method: isolated from a natural source Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium (bacteria) References: UniProt: P15928 #2: Protein | Mass: 36651.688 Da / Num. of mol.: 34 / Mutation: delta169-171 (PAA) / Source method: isolated from a natural source Details: Residues 169-171 (PAA) were deleted on the chromosome. Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium (bacteria) References: UniProt: P0A1J9 #3: Protein | Mass: 37901.066 Da / Num. of mol.: 34 / Source method: isolated from a natural source Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium (bacteria) References: UniProt: P26418 #4: Protein | Mass: 14801.823 Da / Num. of mol.: 102 / Source method: isolated from a natural source Source: (natural) Salmonella enterica subsp. enterica serovar Typhimurium (bacteria) References: UniProt: P26419 |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Intact C34 flagellar C-ring from purified basal bodies, clockwise locked. Type: COMPLEX / Entity ID: all / Source: NATURAL |
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Source (natural) | Organism: Salmonella enterica subsp. enterica serovar Typhimurium (bacteria) |
Buffer solution | pH: 8.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2000 nm / Nominal defocus min: 500 nm |
Image recording | Electron dose: 58.5 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
-Processing
EM software | Name: PHENIX / Version: 1.21rc1_5084 / Category: model refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 5.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 19363 / Symmetry type: POINT | ||||||||||||||||||||||||
Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
Displacement parameters | Biso mean: 404.63 Å2 | ||||||||||||||||||||||||
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