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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-25382 | |||||||||
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Title | Cryo-EM structure of the Achromobacter flagellar filament | |||||||||
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![]() | Bacterial flagella / motility / soil / STRUCTURAL PROTEIN | |||||||||
Function / homology | ![]() bacterial-type flagellum / structural molecule activity / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 3.7 Å | |||||||||
![]() | Kreutzberger MA / Wang F / Egelman EH | |||||||||
Funding support | ![]()
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![]() | ![]() 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 |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 62.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 9.7 KB 9.7 KB | Display Display | ![]() |
Images | ![]() | 82.6 KB | ||
Filedesc metadata | ![]() | 5.2 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 551 KB | Display | ![]() |
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Full document | ![]() | 550.6 KB | Display | |
Data in XML | ![]() | 4.4 KB | Display | |
Data in CIF | ![]() | 5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7sqdMC ![]() 7sn4C ![]() 7sn7C ![]() 7sn9C ![]() 7sqjC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Voxel size | X=Y=Z: 1.06 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Bacterial flagellar filament
Entire | Name: Bacterial flagellar filament |
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Components |
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-Supramolecule #1: Bacterial flagellar filament
Supramolecule | Name: Bacterial flagellar filament / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Flagellin
Macromolecule | Name: Flagellin / type: protein_or_peptide / ID: 1 / Number of copies: 48 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 57.454473 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MAAVINTNYL SLVAQNNLNK SQSSLGTAIE RLSSGLRINS AKDDAAGMAI ANRFTANVRG LTQAARNAND GISLAQTTEG AASEVNTHL QRIRELTVQA SNGSYSQEQL DSVQGEINQR LADIDRISEQ TDFNGVKVLS DSAKPLTLQV GANDGETITL N LSEISVKT ...String: MAAVINTNYL SLVAQNNLNK SQSSLGTAIE RLSSGLRINS AKDDAAGMAI ANRFTANVRG LTQAARNAND GISLAQTTEG AASEVNTHL QRIRELTVQA SNGSYSQEQL DSVQGEINQR LADIDRISEQ TDFNGVKVLS DSAKPLTLQV GANDGETITL N LSEISVKT LGLDGFNVNG KGVTQNRSAT VTDVIAQGGT LQGDGTYKAT TTFNAASAET VLSKLEDGNT VAVGGGATYT YD AAKGNFT YTKTVDTTVG ADVTALANKI KPSSGTISGS YEISTGKSAS FDVDAAGKIT IGGNAAFLNA DGELTTNDAS GAL TQATLD DVLTSVGTEA NSSVTIGGTK YSHSAADELS YTAVATTADV LSAMGSSTAV STVTLGSGIT SAAVTFAIAT TDSN NTWVD NKGELTDIQT FDTSYKINAD TGEVTVVGDN SATAGQYASA DGAKVLVGSD GKLTTETTSA GDKTTDPLKT LDAAF TKLD KLTGELGAVQ NRLESTIANL NNVVNNLSSA RSRIQDADYA TEVSNMSKAQ ILQQAGTSVL AQANQVPQTV LSLLR UniProtKB: Flagellin |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | helical reconstruction |
Aggregation state | filament |
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Sample preparation
Buffer | pH: 7 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Final reconstruction | Applied symmetry - Helical parameters - Δz: 18.9 Å Applied symmetry - Helical parameters - Δ&Phi: -98.4 ° Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric) Resolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 200000 |
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Startup model | Type of model: PDB ENTRY |
Final angle assignment | Type: NOT APPLICABLE |