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- EMDB-40765: Cryo-EM structure of the wild type P. aeruginosa flagellar filament -

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Basic information

Entry
Database: EMDB / ID: EMD-40765
TitleCryo-EM structure of the wild type P. aeruginosa flagellar filament
Map data
Sample
  • Complex: Bacterial flagellar filament
    • Protein or peptide: B-type flagellin
KeywordsBacterial flagellar filament / motility / Pseudomonas / STRUCTURAL PROTEIN / PROTEIN FILAMENT
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)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.2 Å
AuthorsKreutzberger MA / Nedeljkovic M / Egelman EH / Sundberg EJ
Funding support United States, 1 items
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, 2023-
Header (metadata) releaseJun 14, 2023-
Map releaseJun 14, 2023-
UpdateJun 19, 2024-
Current statusJun 19, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_40765.png

Downloads & links

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Map

FileDownload / File: emd_40765.map.gz / Format: CCP4 / Size: 307.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 0.92 Å
Density
Contour LevelBy AUTHOR: 0.075
Minimum - Maximum-0.2227268 - 0.3787366
Average (Standard dev.)0.003666859 (±0.022668026)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions432432432
Spacing432432432
CellA=B=C: 397.44 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_40765_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_40765_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_40765_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Bacterial flagellar filament

EntireName: Bacterial flagellar filament
Components
  • Complex: Bacterial flagellar filament
    • Protein or peptide: B-type flagellin

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Supramolecule #1: Bacterial flagellar filament

SupramoleculeName: Bacterial flagellar filament / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Pseudomonas aeruginosa PAO1 (bacteria)

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Macromolecule #1: B-type flagellin

MacromoleculeName: B-type flagellin / type: protein_or_peptide / ID: 1 / Number of copies: 33 / Enantiomer: LEVO
Source (natural)Organism: Pseudomonas aeruginosa PAO1 (bacteria)
Molecular weightTheoretical: 48.872355 KDa
SequenceString: VNTNIASLNT QRNLNASSND LNTSLQRLTT GYRINSAKDD AAGLQISNRL SNQISGLNVA TRNANDGISL AQTAEGALQQ STNILQRIR DLALQSANGS NSDADRAALQ KEVAAQQAEL TRISDTTTFG GRKLLDGSFG TTSFQVGSNA YETIDISLQN A SASAIGSY ...String:
VNTNIASLNT QRNLNASSND LNTSLQRLTT GYRINSAKDD AAGLQISNRL SNQISGLNVA TRNANDGISL AQTAEGALQQ STNILQRIR DLALQSANGS NSDADRAALQ KEVAAQQAEL TRISDTTTFG GRKLLDGSFG TTSFQVGSNA YETIDISLQN A SASAIGSY QVGSNGAGTV ASVAGTATAS GIASGTVNLV GGGQVKNIAI AAGDSAKAIA EKMDGAIPNL SARARTVFTA DV SGVTGGS LNFDVTVGSN TVSLAGVTST QDLADQLNSN SSKLGITASI NDKGVLTITS ATGENVKFGA QTGTATAGQV AVK VQGSDG KFEAAAKNVV AAGTAATTTI VTGYVQLNSP TAYSVSGTGT QASQVFGNAS AAQKSSVASV DISTADGAQN AIAV VDNAL AAIDAQRADL AAVQNRFKNT IDNLTNISEN ATNARSRIKD TDFAAETAAL SKNQVLQQAG TAILAQANQL PQAVL SLLR

UniProtKB: B-type flagellin

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation statefilament

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Sample preparation

BufferpH: 7.2
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS GLACIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm

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Image processing

Startup modelType of model: EMDB MAP
EMDB ID:

27064

Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 29945
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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