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- EMDB-25213: Cryo-EM structure of the enteropathogenic E. coli O127:H6 flagell... -

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Basic information

Entry
Database: EMDB / ID: EMD-25213
TitleCryo-EM structure of the enteropathogenic E. coli O127:H6 flagellar filament
Map data
Sample
  • Complex: Bacterial flagellar filament
    • Protein or peptide: Flagellin
KeywordsBacteria flagellar filament / motility / flagellar polymorphism / STRUCTURAL PROTEIN
Function / homology:
Function and homology information
Biological speciesEscherichia coli O127:H6 (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.2 Å
AuthorsKreutzberger MAB / Chatterjee S
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM122510 United States
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-
UpdateJun 5, 2024-
Current statusJun 5, 2024Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.203
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.203
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7sn7
  • Surface level: 0.203
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-7sn7
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_25213.png

Downloads & links

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Map

FileDownload / File: emd_25213.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.08 Å
Density
Contour LevelBy AUTHOR: 0.203 / Movie #1: 0.203
Minimum - Maximum-1.0468874 - 1.8074155
Average (Standard dev.)0.003780077 (±0.070000455)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 414.72003 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.081.081.08
M x/y/z384384384
origin x/y/z0.0000.0000.000
length x/y/z414.720414.720414.720
α/β/γ90.00090.00090.000
start NX/NY/NZ138136120
NX/NY/NZ121111179
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS384384384
D min/max/mean-1.0471.8070.004

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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 O127:H6 (bacteria)

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Macromolecule #1: Flagellin

MacromoleculeName: Flagellin / type: protein_or_peptide / ID: 1 / Number of copies: 23 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli O127:H6 (bacteria)
Molecular weightTheoretical: 56.13973 KDa
SequenceString: QVINTNSLSL ITQNNINKNQ SALSSSIERL SSGLRINSAK DDAAGQAIAN RFTSNIKGLT QAARNANDGI SVAQTTEGAL SEINNNLQR IRELTVQAST GTNSDSDLDS IQDEIKSRLD EIDRVSGQTQ FNGVNVLAKD GSMKIQVGAN DGQTITIDLK K IDSDTLGL ...String:
QVINTNSLSL ITQNNINKNQ SALSSSIERL SSGLRINSAK DDAAGQAIAN RFTSNIKGLT QAARNANDGI SVAQTTEGAL SEINNNLQR IRELTVQAST GTNSDSDLDS IQDEIKSRLD EIDRVSGQTQ FNGVNVLAKD GSMKIQVGAN DGQTITIDLK K IDSDTLGL NGFNVNGKGE TANTAATLKD MSGFTAAAAP GGTVGVTQYT DKSAVASSVD ILNAVAGADG NKVTTSADVG FG TPAAAVT YTYNKDTNSY SAASDDISSA NLAAFLNPQA RDTTKATVTI GGKDQDVNID KSGNLTAADD GAVLYMDATG NLT KNNAGG DTQATLAKVA TATGAKAATI QTDKGTFTSD GTAFDGASMS IDANTFANAV KNDTYTATVG AKTYSVTTGS AAAD TAYMS NGVLSDTPPT YYAQADGSIT TTEDAAAGKL VYKGSDGKLT TDTTSKAEST SDPLAALDDA ISQIDKFRSS LGAVQ NRLD SAVTNLNNTT TNLSEAQSRI QDADYATEVS NMSKAQIIQQ AGNSVLAKAN QVPQQVLSLL QG

UniProtKB: UNIPROTKB: A0A2D0NRN6

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

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Image processing

Startup modelType of model: PDB ENTRY
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 269269
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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