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- PDB-8sug: Cryo-EM structure of the wild type P. aeruginosa flagellar filament -

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Basic information

Entry
Database: PDB / ID: 8sug
TitleCryo-EM structure of the wild type P. aeruginosa flagellar filament
ComponentsB-type flagellin
KeywordsSTRUCTURAL PROTEIN / PROTEIN FILAMENT / Bacterial flagellar filament / motility / Pseudomonas
Function / homology
Function and homology information


bacterial-type flagellum / bacterial-type flagellum-dependent cell motility / structural molecule activity / extracellular region
Similarity search - Function
Flagellin hook, IN motif / Flagellin hook IN motif / Flagellin, C-terminal domain, subdomain 2 / 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
Biological speciesPseudomonas aeruginosa PAO1 (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.2 Å
AuthorsKreutzberger, M.A. / Nedeljkovic, M. / Egelman, E.H. / Sundberg, E.J.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM122510 United States
CitationJournal: PLoS Pathog / Year: 2023
Title: An unbroken network of interactions connecting flagellin domains is required for motility in viscous environments.
Authors: Marko Nedeljković / Mark A B Kreutzberger / Sandra Postel / Daniel Bonsor / Yingying Xing / Neil Jacob / William J Schuler / Edward H Egelman / Eric J Sundberg /
Abstract: In its simplest form, bacterial flagellar filaments are composed of flagellin proteins with just two helical inner domains, which together comprise the filament core. Although this minimal filament ...In its simplest form, bacterial flagellar filaments are composed of flagellin proteins with just two helical inner domains, which together comprise the filament core. Although this minimal filament is sufficient to provide motility in many flagellated bacteria, most bacteria produce flagella composed of flagellin proteins with one or more outer domains arranged in a variety of supramolecular architectures radiating from the inner core. Flagellin outer domains are known to be involved in adhesion, proteolysis and immune evasion but have not been thought to be required for motility. Here we show that in the Pseudomonas aeruginosa PAO1 strain, a bacterium that forms a ridged filament with a dimerization of its flagellin outer domains, motility is categorically dependent on these flagellin outer domains. Moreover, a comprehensive network of intermolecular interactions connecting the inner domains to the outer domains, the outer domains to one another, and the outer domains back to the inner domain filament core, is required for motility. This inter-domain connectivity confers PAO1 flagella with increased stability, essential for its motility in viscous environments. Additionally, we find that such ridged flagellar filaments are not unique to Pseudomonas but are, instead, present throughout diverse bacterial phyla.
History
DepositionMay 12, 2023Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 14, 2023Provider: repository / Type: Initial release
Revision 1.1Jun 19, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: B-type flagellin
B: B-type flagellin
C: B-type flagellin
D: B-type flagellin
E: B-type flagellin
F: B-type flagellin
G: B-type flagellin
H: B-type flagellin
I: B-type flagellin
J: B-type flagellin
K: B-type flagellin
L: B-type flagellin
M: B-type flagellin
N: B-type flagellin
O: B-type flagellin
P: B-type flagellin
Q: B-type flagellin
R: B-type flagellin
S: B-type flagellin
T: B-type flagellin
U: B-type flagellin
V: B-type flagellin
W: B-type flagellin
X: B-type flagellin
Y: B-type flagellin
Z: B-type flagellin
a: B-type flagellin
b: B-type flagellin
c: B-type flagellin
d: B-type flagellin
e: B-type flagellin
f: B-type flagellin
g: B-type flagellin


Theoretical massNumber of molelcules
Total (without water)1,612,78833
Polymers1,612,78833
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein ...
B-type flagellin


Mass: 48872.355 Da / Num. of mol.: 33 / Source method: isolated from a natural source / Source: (natural) Pseudomonas aeruginosa PAO1 (bacteria) / References: UniProt: P72151

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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: Bacterial flagellar filament / Type: COMPLEX / Entity ID: all / Source: NATURAL
Source (natural)Organism: Pseudomonas aeruginosa PAO1 (bacteria)
Buffer solutionpH: 7.2
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

MicroscopyModel: TFS GLACIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 3000 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k)

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Processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 29945 / Symmetry type: POINT

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