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- PDB-9gsx: Campylobacter hook-filament junction-cap complex -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 9gsx
TitleCampylobacter hook-filament junction-cap complex
Components
  • Flagellar hook-associated protein 1
  • Flagellar hook-associated protein 2
  • Flagellin
KeywordsTRANSPORT PROTEIN / Campylobacter jejuni / flagellar cap / hook-filament junction / FliD / FlgK / FlgL / flagella
Function / homology
Function and homology information


bacterial-type flagellum filament cap / bacterial-type flagellum hook / bacterial-type flagellum / bacterial-type flagellum assembly / bacterial-type flagellum-dependent cell motility / cell adhesion / structural molecule activity / extracellular region
Similarity search - Function
Flagellar hook-associated protein 1 / : / Flagellar hook-associated protein FlgK helical domain / Flagellar hook-associated protein 2, N-terminal / Flagellar hook-associated protein 2, C-terminal / Flagellar hook-associated protein 2 / Flagellar hook-associated protein 2 N-terminus / Flagellar hook-associated protein 2 C-terminus / Flagellin hook, IN motif / Flagellin hook IN motif ...Flagellar hook-associated protein 1 / : / Flagellar hook-associated protein FlgK helical domain / Flagellar hook-associated protein 2, N-terminal / Flagellar hook-associated protein 2, C-terminal / Flagellar hook-associated protein 2 / Flagellar hook-associated protein 2 N-terminus / Flagellar hook-associated protein 2 C-terminus / Flagellin hook, IN motif / Flagellin hook IN motif / Flagellar basal body rod protein, N-terminal / Flagellar basal-body/hook protein, C-terminal domain / Flagella basal body rod protein / Flagellar basal body rod FlgEFG protein C-terminal / Flagellin, C-terminal domain / Bacterial flagellin C-terminal helical region / Flagellin / Flagellin, N-terminal domain / Bacterial flagellin N-terminal helical region
Similarity search - Domain/homology
Flagellin / Flagellar hook-associated protein 1 / Flagellar hook-associated protein 2
Similarity search - Component
Biological speciesCampylobacter jejuni (Campylobacter)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 6.5 Å
AuthorsQin, K. / Gonzalez-Rodriguez, N. / Shmakova, E. / Beeby, M. / Bergeron, J.R.C.
Funding support United Kingdom, France, 2items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom)MR/V000799/1 United Kingdom
Human Frontier Science Program (HFSP)RGP0028/2021-HOCHBERG France
CitationJournal: To Be Published
Title: Structure of the complete extracellular bacterial flagellum reveals mechanism for flagellin incorporation
Authors: Qin, K. / Einenkel, R. / Al-Otaibi, N.S. / Schmidt, J. / Mann, D. / Drobnic, T. / Cohen, E.J. / Gonzalez-Rodriguez, N. / Harrowell, J. / Shmakova, E. / Beeby, M. / Erhardt, M. / Bergeron, J.R.C.
History
DepositionSep 16, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 9, 2025Provider: repository / Type: Initial release
Revision 1.0Apr 9, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Apr 9, 2025Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Apr 9, 2025Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Apr 9, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Apr 9, 2025Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Flagellin
B: Flagellin
C: Flagellin
D: Flagellin
E: Flagellin
F: Flagellin
G: Flagellin
H: Flagellin
I: Flagellin
J: Flagellin
K: Flagellin
L: Flagellar hook-associated protein 1
M: Flagellar hook-associated protein 1
N: Flagellar hook-associated protein 1
O: Flagellar hook-associated protein 1
P: Flagellar hook-associated protein 1
Q: Flagellar hook-associated protein 1
R: Flagellar hook-associated protein 1
S: Flagellar hook-associated protein 1
T: Flagellar hook-associated protein 1
U: Flagellar hook-associated protein 1
V: Flagellar hook-associated protein 1
W: Flagellar hook-associated protein 2
X: Flagellar hook-associated protein 2
Y: Flagellar hook-associated protein 2
Z: Flagellar hook-associated protein 2
a: Flagellar hook-associated protein 2


Theoretical massNumber of molelcules
Total (without water)1,990,07227
Polymers1,990,07227
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein
Flagellin


Mass: 82047.000 Da / Num. of mol.: 11 / Source method: isolated from a natural source / Source: (natural) Campylobacter jejuni (Campylobacter) / References: UniProt: A0A5T0F6D4
#2: Protein
Flagellar hook-associated protein 1


Mass: 67121.469 Da / Num. of mol.: 11 / Source method: isolated from a natural source / Source: (natural) Campylobacter jejuni (Campylobacter) / References: UniProt: A0A5Z5AC44
#3: Protein
Flagellar hook-associated protein 2 / HAP2 / Filament cap protein / Flagellar cap protein


Mass: 69843.852 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) Campylobacter jejuni (Campylobacter) / References: UniProt: Q9PHW6
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: FILAMENT / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Hook-filament junction-cap complex in Campylobacter jejuni
Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: all / Source: NATURAL
Source (natural)Organism: Campylobacter jejuni (Campylobacter)
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 3000 nm / Nominal defocus min: 1500 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K2 BASE (4k x 4k)

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Processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 6.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 15077 / Symmetry type: POINT

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