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- EMDB-25211: Cryo-EM structure of the enterohemorrhagic E. coli O157:H7 flagel... -

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Basic information

Entry
Database: EMDB / ID: EMD-25211
TitleCryo-EM structure of the enterohemorrhagic E. coli O157:H7 flagellar filament
Map data
Sample
  • Complex: Bacterial flagellar filament
    • Protein or peptide: Flagellin
Function / homology
Function and homology information


bacterial-type flagellum / structural molecule activity / extracellular region
Similarity search - Function
Flagellin, H7-serospecific domain / Flagellin protein / Flagellin, C-terminal domain, subdomain 2 / Bacterial flagellin C-terminal helical region / Flagellin / Flagellin, N-terminal domain / Bacterial flagellin N-terminal helical region
Similarity search - Domain/homology
Biological speciesEscherichia coli (E. coli) / Escherichia coli O157:H7 (bacteria)
Methodhelical reconstruction / cryo EM / Resolution: 3.6 Å
AuthorsKreutzberger MAB / Wang F / Egelman EH
Funding support1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM122510
CitationJournal: Nat Commun / Year: 2022
Title: Flagellin outer domain dimerization modulates motility in pathogenic and soil bacteria from viscous environments.
Authors: Mark A B Kreutzberger / Richard C Sobe / Amber B Sauder / Sharanya Chatterjee / Alejandro Peña / Fengbin Wang / Jorge A Giron / Volker Kiessling / Tiago R D Costa / Vincent P Conticello / ...Authors: Mark A B Kreutzberger / Richard C Sobe / Amber B Sauder / Sharanya Chatterjee / Alejandro Peña / Fengbin Wang / Jorge A Giron / Volker Kiessling / Tiago R D Costa / Vincent P Conticello / Gad Frankel / Melissa M Kendall / Birgit E Scharf / Edward H Egelman /
Abstract: Flagellar filaments function as the propellers of the bacterial flagellum and their supercoiling is key to motility. The outer domains on the surface of the filament are non-critical for motility in ...Flagellar filaments function as the propellers of the bacterial flagellum and their supercoiling is key to motility. The outer domains on the surface of the filament are non-critical for motility in many bacteria and their structures and functions are not conserved. Here, we show the atomic cryo-electron microscopy structures for flagellar filaments from enterohemorrhagic Escherichia coli O157:H7, enteropathogenic E. coli O127:H6, Achromobacter, and Sinorhizobium meliloti, where the outer domains dimerize or tetramerize to form either a sheath or a screw-like surface. These dimers are formed by 180° rotations of half of the outer domains. The outer domain sheath (ODS) plays a role in bacterial motility by stabilizing an intermediate waveform and prolonging the tumbling of E. coli cells. Bacteria with these ODS and screw-like flagellar filaments are commonly found in soil and human intestinal environments of relatively high viscosity suggesting a role for the dimerization in these environments.
History
DepositionOct 27, 2021-
Header (metadata) releaseMar 16, 2022-
Map releaseMar 16, 2022-
UpdateMar 30, 2022-
Current statusMar 30, 2022Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.0064
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.0064
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7sn4
  • Surface level: 0.0064
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-7sn4
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_25211.png

Downloads & links

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Map

FileDownload / File: emd_25211.map.gz / Format: CCP4 / Size: 200 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.08 Å
Density
Contour LevelBy AUTHOR: 0.0064 / Movie #1: 0.0064
Minimum - Maximum-0.015974637 - 0.03552642
Average (Standard dev.)0.0007391037 (±0.0027183515)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320512
Spacing320320512
CellA: 345.6 Å / B: 345.6 Å / C: 552.96 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.081.081.08
M x/y/z320320512
origin x/y/z0.0000.0000.000
length x/y/z345.600345.600552.960
α/β/γ90.00090.00090.000
start NX/NY/NZ138136120
NX/NY/NZ121111179
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS320320512
D min/max/mean-0.0160.0360.001

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Supplemental data

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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: 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: Escherichia coli (E. coli)

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Macromolecule #1: Flagellin

MacromoleculeName: Flagellin / type: protein_or_peptide / ID: 1 / Number of copies: 44 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli O157:H7 (bacteria) / Strain: O157:H7 str 86-24
Molecular weightTheoretical: 60.000172 KDa
Recombinant expressionOrganism: Escherichia coli O157:H7 (bacteria)
SequenceString: MAQVINTNSL SLITQNNINK NQSALSSSIE RLSSGLRINS AKDDAAGQAI ANRFTSNIKG LTQAARNAND GISVAQTTEG ALSEINNNL QRIRELTVQA TTGTNSDSDL DSIQDEIKSR LDEIDRVSGQ TQFNGVNVLA KDGSMKIQVG ANDGETITID L KKIDSDTL ...String:
MAQVINTNSL SLITQNNINK NQSALSSSIE RLSSGLRINS AKDDAAGQAI ANRFTSNIKG LTQAARNAND GISVAQTTEG ALSEINNNL QRIRELTVQA TTGTNSDSDL DSIQDEIKSR LDEIDRVSGQ TQFNGVNVLA KDGSMKIQVG ANDGETITID L KKIDSDTL GLNGFNVNGK GTITNKAATV SDLTSAGAKL NTTTGLYDLK TENTLLTTDA AFDKLGNGDK VTVGGVDYTY NA KSGDFTT TKSTAGTGVD AAAQAADSAS KRDALAATLH ADVGKSVNGS YTTKDGTVSF ETDSAGNITI GGSQAYVDDA GNL TTNNAG SAAKADMKAL LKAASEGSDG ASLTFNGTEY TIAKATPATT TPVAPLIPGG ITYQATVSKD VVLSETKAAA ATSS ITFNS GVLSKTIGFT AGESSDAAKS YVDDKGGITN VADYTVSYSV NKDNGSVTVA GYASATDTNK DYAPAIGTAV NVNSA GKIT TETTSAGSAT TNPLAALDDA ISSIDKFRSS LGAIQNRLDS AVTNLNNTTT NLSEAQSRIQ DADYATEVSN MSKAQI IQQ AGNSVLAKAN QVPQQVLSLL QG

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Experimental details

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Structure determination

Methodcryo EM
Processinghelical reconstruction
Aggregation statefilament

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Sample preparation

BufferpH: 7.2
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

5wjy

Final angle assignmentType: NOT APPLICABLE
Final reconstructionApplied symmetry - Helical parameters - Δz: 130.78 Å
Applied symmetry - Helical parameters - Δ&Phi: 9.68 °
Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric)
Resolution.type: BY AUTHOR / Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 200000

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