|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.|
|Sample||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.|
|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.
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_20830.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.32 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-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.|
Number of components: 1
-Component #1: protein, PrgH and PrgK, the protein components of the inner rings...
|Protein||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.|
Recombinant expression: No
|Source||Species: Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||pH: 7.5|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 48 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
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