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- PDB-7e82: Cryo-EM structure of the flagellar rod with partial hook from Sal... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7.0E+82 | |||||||||||||||||||||
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Title | Cryo-EM structure of the flagellar rod with partial hook from Salmonella | |||||||||||||||||||||
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![]() | MOTOR PROTEIN / Flagella / Rod | |||||||||||||||||||||
Function / homology | ![]() bacterial-type flagellum basal body, rod / bacterial-type flagellum basal body, distal rod / bacterial-type flagellum basal body, MS ring / bacterial-type flagellum basal body / bacterial-type flagellum-dependent swarming motility / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / structural molecule activity / plasma membrane Similarity search - Function | |||||||||||||||||||||
Biological species | ![]() | |||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||||||||||||||
![]() | Tan, J.X. / Chang, S.H. / Wang, X.F. / Xu, C.H. / Zhou, Y. / Zhang, X. / Zhu, Y.Q. | |||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis of assembly and torque transmission of the bacterial flagellar motor. Authors: Jiaxing Tan / Xing Zhang / Xiaofei Wang / Caihuang Xu / Shenghai Chang / Hangjun Wu / Ting Wang / Huihui Liang / Haichun Gao / Yan Zhou / Yongqun Zhu / ![]() Abstract: The bacterial flagellar motor is a supramolecular protein machine that drives rotation of the flagellum for motility, which is essential for bacterial survival in different environments and a key ...The bacterial flagellar motor is a supramolecular protein machine that drives rotation of the flagellum for motility, which is essential for bacterial survival in different environments and a key determinant of pathogenicity. The detailed structure of the flagellar motor remains unknown. Here we present an atomic-resolution cryoelectron microscopy (cryo-EM) structure of the bacterial flagellar motor complexed with the hook, consisting of 175 subunits with a molecular mass of approximately 6.3 MDa. The structure reveals that 10 peptides protruding from the MS ring with the FlgB and FliE subunits mediate torque transmission from the MS ring to the rod and overcome the symmetry mismatch between the rotational and helical structures in the motor. The LP ring contacts the distal rod and applies electrostatic forces to support its rotation and torque transmission to the hook. This work provides detailed molecular insights into the structure, assembly, and torque transmission mechanisms of the flagellar motor. | |||||||||||||||||||||
History |
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Structure visualization
Movie |
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 2.1 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 31008MC ![]() 7cblC ![]() 7cbmC ![]() 7cg0C ![]() 7cg4C ![]() 7cg7C ![]() 7cgbC ![]() 7cgoC ![]() 7e80C ![]() 7e81C M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
-Flagellar basal-body rod protein ... , 3 types, 35 molecules ABCDEFGHIJKLMNOPQRSTUVWXabcdef...
#1: Protein | Mass: 27784.807 Da / Num. of mol.: 24 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P0A1J3 #2: Protein | Mass: 26121.223 Da / Num. of mol.: 5 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P16323 #5: Protein | Mass: 13991.889 Da / Num. of mol.: 6 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P0A1I7 |
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-Flagellar MS ring ... , 2 types, 10 molecules 0123456798
#3: Protein/peptide | Mass: 1294.587 Da / Num. of mol.: 5 / Source method: isolated from a natural source Source: (natural) ![]() #4: Protein/peptide | Mass: 1998.195 Da / Num. of mol.: 5 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P15928 |
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-Protein , 3 types, 22 molecules lmoknqrstuvDADBDCDDDEDFDGDHDIDJDK
#6: Protein | Mass: 15145.061 Da / Num. of mol.: 5 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P16437 #7: Protein | Mass: 11087.662 Da / Num. of mol.: 6 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P26462 #8: Protein | Mass: 42233.152 Da / Num. of mol.: 11 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P0A1J1 |
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-Details
Sequence details | The complex was purified from the natural source and the sequence of Flagellar M-ring protein is ...The complex was purified from the natural source and the sequence of Flagellar M-ring protein is listed below: MSATASTATQ |
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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 |
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Sample preparation
Component | Name: Flagellar motor-hook / Type: COMPLEX / Entity ID: all / Source: NATURAL | ||||||||||||||||||||
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Molecular weight | Experimental value: NO | ||||||||||||||||||||
Source (natural) | Organism: ![]() | ||||||||||||||||||||
Buffer solution | pH: 8 | ||||||||||||||||||||
Buffer component |
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Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||
Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 | ||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 295 K / Details: blot for 6 seconds before plunging |
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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: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 47 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 102044 / Symmetry type: POINT |