[English] 日本語
Yorodumi- EMDB-20830: Cryo-EM reconstruction of the inner membrane rings containing the... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-20830 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Cryo-EM reconstruction of the inner membrane rings containing the core components of the export apparatus and associated membranes of the needle complex from Salmonella typhimurium type III secretion system. | |||||||||
Map data | ||||||||||
Sample |
| |||||||||
Biological species | Salmonella enterica subsp. enterica serovar Typhimurium (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.93 Å | |||||||||
Authors | Butan C / Galan J | |||||||||
Funding support | 1 items
| |||||||||
Citation | Journal: Proc Natl Acad Sci U S A / Year: 2019 Title: High-resolution view of the type III secretion export apparatus in situ reveals membrane remodeling and a secretion pathway. Authors: Carmen Butan / Maria Lara-Tejero / Wenwei Li / Jun Liu / Jorge E Galán / Abstract: Type III protein secretion systems are essential virulence factors for many important pathogenic bacteria. The entire protein secretion machine is composed of several substructures that organize into ...Type III protein secretion systems are essential virulence factors for many important pathogenic bacteria. The entire protein secretion machine is composed of several substructures that organize into a holostructure or injectisome. The core component of the injectisome is the needle complex, which houses the export apparatus that serves as a gate for the passage of the secreted proteins through the bacterial inner membrane. Here, we describe a high-resolution structure of the export apparatus of the type III secretion system in association with the needle complex and the underlying bacterial membrane, both in isolation and in situ. We show the precise location of the core export apparatus components within the injectisome and bacterial envelope and demonstrate that their deployment results in major membrane remodeling and thinning, which may be central for the protein translocation process. We also show that InvA, a critical export apparatus component, forms a multiring cytoplasmic conduit that provides a pathway for the type III secretion substrates to reach the entrance of the export gate. Combined with structure-guided mutagenesis, our studies provide major insight into potential mechanisms of protein translocation and injectisome assembly. | |||||||||
History |
|
-Structure visualization
Movie |
Movie viewer |
---|---|
Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_20830.map.gz | 65.5 MB | EMDB map data format | |
---|---|---|---|---|
Header (meta data) | emd-20830-v30.xml emd-20830.xml | 9.1 KB 9.1 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_20830_fsc.xml | 10 KB | Display | FSC data file |
Images | emd_20830.png | 344.6 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-20830 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-20830 | HTTPS FTP |
-Validation report
Summary document | emd_20830_validation.pdf.gz | 78.1 KB | Display | EMDB validaton report |
---|---|---|---|---|
Full document | emd_20830_full_validation.pdf.gz | 77.2 KB | Display | |
Data in XML | emd_20830_validation.xml.gz | 495 B | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-20830 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-20830 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
---|
-Map
File | Download / File: emd_20830.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Voxel size | X=Y=Z: 1.32 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
|
-Supplemental data
-Sample components
-Entire : PrgH and PrgK, the protein components of the inner rings of the S...
Entire | Name: PrgH and PrgK, the protein components of the inner rings of the Salmonella's needle complex, in complex with the core components of the export apparatus and associated membranes. |
---|---|
Components |
|
-Supramolecule #1: PrgH and PrgK, the protein components of the inner rings of the S...
Supramolecule | Name: PrgH and PrgK, the protein components of the inner rings of the Salmonella's needle complex, in complex with the core components of the export apparatus and associated membranes. type: complex / ID: 1 / Parent: 0 |
---|---|
Source (natural) | Organism: Salmonella enterica subsp. enterica serovar Typhimurium (bacteria) |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
---|---|
Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 48.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |