[English] 日本語
![](img/lk-miru.gif)
- EMDB-25386: Cryo-EM structure of the seam subunits of the enteropathogenic E.... -
+
Open data
-
Basic information
Entry | Database: EMDB / ID: EMD-25386 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Cryo-EM structure of the seam subunits of the enteropathogenic E. coli O127:H6 flagellar filament | |||||||||
![]() | ||||||||||
![]() |
| |||||||||
![]() | Bacteria flagellar filament / motility / flagellar polymorphism / STRUCTURAL PROTEIN | |||||||||
Function / homology | ![]() bacterial-type flagellum / structural molecule activity / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 6.3 Å | |||||||||
![]() | Kreutzberger MAB / Chatterjee S / Frankel G / Egelman EH | |||||||||
Funding support | ![]()
| |||||||||
![]() | ![]() 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 |
|
-
Structure visualization
Movie |
![]() |
---|---|
Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
-
Downloads & links
-EMDB archive
Map data | ![]() | 203.2 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 9.7 KB 9.7 KB | Display Display | ![]() |
Images | ![]() | 92.1 KB | ||
Filedesc metadata | ![]() | 5.1 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 532.6 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 532.2 KB | Display | |
Data in XML | ![]() | 7.2 KB | Display | |
Data in CIF | ![]() | 8.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7sqjMC ![]() 7sn4C ![]() 7sn7C ![]() 7sn9C ![]() 7sqdC M: atomic model generated by this map C: citing same article ( |
---|---|
Similar structure data |
-
Links
EMDB pages | ![]() ![]() |
---|
-
Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Voxel size | X=Y=Z: 1.08 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
|
-Supplemental data
-
Sample components
-Entire : Bacterial flagellar filament
Entire | Name: Bacterial flagellar filament |
---|---|
Components |
|
-Supramolecule #1: Bacterial flagellar filament
Supramolecule | Name: Bacterial flagellar filament / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
---|---|
Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Flagellin
Macromolecule | Name: Flagellin / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 56.342008 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MAQVINTNSL SLITQNNINK NQSALSSSIE RLSSGLRINS AKDDAAGQAI ANRFTSNIKG LTQAARNAND GISVAQTTEG ALSEINNNL QRIRELTVQA STGTNSDSDL DSIQDEIKSR LDEIDRVSGQ TQFNGVNVLA KDGSMKIQVG ANDGQTITID L KKIDSDTL ...String: MAQVINTNSL SLITQNNINK NQSALSSSIE RLSSGLRINS AKDDAAGQAI ANRFTSNIKG LTQAARNAND GISVAQTTEG ALSEINNNL QRIRELTVQA STGTNSDSDL DSIQDEIKSR LDEIDRVSGQ TQFNGVNVLA KDGSMKIQVG ANDGQTITID L KKIDSDTL GLNGFNVNGK GETANTAATL KDMSGFTAAA APGGTVGVTQ YTDKSAVASS VDILNAVAGA DGNKVTTSAD VG FGTPAAA VTYTYNKDTN SYSAASDDIS SANLAAFLNP QARDTTKATV TIGGKDQDVN IDKSGNLTAA DDGAVLYMDA TGN LTKNNA GGDTQATLAK VATATGAKAA TIQTDKGTFT SDGTAFDGAS MSIDANTFAN AVKNDTYTAT VGAKTYSVTT GSAA ADTAY MSNGVLSDTP PTYYAQADGS ITTTEDAAAG KLVYKGSDGK LTTDTTSKAE STSDPLAALD DAISQIDKFR SSLGA VQNR LDSAVTNLNN TTTNLSEAQS RIQDADYATE VSNMSKAQII QQAGNSVLAK ANQVPQQVLS LLQG UniProtKB: Flagellin |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | single particle reconstruction |
Aggregation state | filament |
-
Sample preparation
Buffer | pH: 7.2 |
---|---|
Vitrification | Cryogen name: ETHANE |
-
Electron microscopy
Microscope | TFS KRIOS |
---|---|
Image recording | Film or detector model: GATAN K3 (6k 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 |
-
Image processing
Startup model | Type of model: PDB ENTRY |
---|---|
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 6.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 60359 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |