+Open data
-Basic information
Entry | Database: PDB / ID: 6ykm | |||||||||
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Title | Structure of C. jejuni MotAB | |||||||||
Components |
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Keywords | MEMBRANE PROTEIN / Bacterial flagellar motor / stator unit / locomotion / proton transport / ion transport | |||||||||
Function / homology | Function and homology information bacterial-type flagellum-dependent swarming motility / chemotaxis / plasma membrane Similarity search - Function | |||||||||
Biological species | Campylobacter jejuni subsp. jejuni serotype O:23/36 (Campylobacter) | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å | |||||||||
Authors | Santiveri, M. / Roa-Eguiara, A. / Taylor, N.M.I. | |||||||||
Funding support | Denmark, 2items
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Citation | Journal: Cell / Year: 2020 Title: Structure and Function of Stator Units of the Bacterial Flagellar Motor. Authors: Mònica Santiveri / Aritz Roa-Eguiara / Caroline Kühne / Navish Wadhwa / Haidai Hu / Howard C Berg / Marc Erhardt / Nicholas M I Taylor / Abstract: Many bacteria use the flagellum for locomotion and chemotaxis. Its bidirectional rotation is driven by a membrane-embedded motor, which uses energy from the transmembrane ion gradient to generate ...Many bacteria use the flagellum for locomotion and chemotaxis. Its bidirectional rotation is driven by a membrane-embedded motor, which uses energy from the transmembrane ion gradient to generate torque at the interface between stator units and rotor. The structural organization of the stator unit (MotAB), its conformational changes upon ion transport, and how these changes power rotation of the flagellum remain unknown. Here, we present ~3 Å-resolution cryoelectron microscopy reconstructions of the stator unit in different functional states. We show that the stator unit consists of a dimer of MotB surrounded by a pentamer of MotA. Combining structural data with mutagenesis and functional studies, we identify key residues involved in torque generation and present a detailed mechanistic model for motor function and switching of rotational direction. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6ykm.cif.gz | 242.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6ykm.ent.gz | 191.3 KB | Display | PDB format |
PDBx/mmJSON format | 6ykm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yk/6ykm ftp://data.pdbj.org/pub/pdb/validation_reports/yk/6ykm | HTTPS FTP |
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-Related structure data
Related structure data | 10828MC 6ykpC 6ykrC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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-Components
#1: Protein | Mass: 28195.816 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) (Campylobacter) Strain: 81-176 / Gene: CJJ81176_0359 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A0H3PAV1 #2: Protein | Mass: 32149.244 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) (Campylobacter) Strain: 81-176 / Gene: CJJ81176_0358 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A0H3PBX6 #3: Water | ChemComp-HOH / | |
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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: Stator unit MotAB / Type: COMPLEX Details: The stator unit consists of a dimer of MotB surrounded by a pentamer of MotA Entity ID: #1-#2 / Source: RECOMBINANT |
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Source (natural) | Organism: Campylobacter jejuni subsp. jejuni 81-176 (Campylobacter) |
Source (recombinant) | Organism: Escherichia coli (E. coli) / Strain: C43(DE3) |
Buffer solution | pH: 8 |
Specimen | Conc.: 0.65 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid type: Quantifoil R2/1 |
Vitrification | Instrument: FEI VITROBOT MARK IV / 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 FIELD |
Image recording | Electron dose: 40.84 e/Å2 / Detector mode: COUNTING / Film or detector model: FEI FALCON III (4k x 4k) |
-Processing
EM software | Name: RELION / Version: 3 / Category: 3D reconstruction | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 278762 / Num. of class averages: 1 / Symmetry type: POINT | ||||||||||||||||||||||||
Refinement | Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
Displacement parameters | Biso mean: 41.93 Å2 | ||||||||||||||||||||||||
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