|Entry||Database: EMDB / ID: EMD-20046|
|Title||Structure of Salmonella type III secretion system needle filamentType three secretion system|
|Map data||Type three secretion system|
|Sample||filament structure of PrgI needle attached to the base:|
|Function / homology||Type III secretion system, needle protein / Type III secretion, needle-protein-like / Type III secretion, needle-protein-like superfamily / type III protein secretion system complex / protein secretion by the type III secretion system / pathogenesis / identical protein binding / Type III secretion system apparatus / Protein PrgI|
Function and homology information
|Biological species||Salmonella typhimurium (strain SL1344) (bacteria)|
|Method||helical reconstruction / cryo EM / Resolution: 3.7 Å|
|Authors||Guo EZ / Galan JE|
|Funding support|| United States, 1 items |
|Citation||Journal: PLoS Biol. / Year: 2019|
Title: A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion.
Authors: Emily Z Guo / Daniel C Desrosiers / Jan Zalesak / James Tolchard / Mélanie Berbon / Birgit Habenstein / Thomas Marlovits / Antoine Loquet / Jorge E Galán /
Abstract: Type III protein-secretion machines are essential for the interactions of many pathogenic or symbiotic bacterial species with their respective eukaryotic hosts. The core component of these machines ...Type III protein-secretion machines are essential for the interactions of many pathogenic or symbiotic bacterial species with their respective eukaryotic hosts. The core component of these machines is the injectisome, a multiprotein complex that mediates the selection of substrates, their passage through the bacterial envelope, and ultimately their delivery into eukaryotic target cells. The injectisome is composed of a large cytoplasmic complex or sorting platform, a multiring base embedded in the bacterial envelope, and a needle-like filament that protrudes several nanometers from the bacterial surface and is capped at its distal end by the tip complex. A characteristic feature of these machines is that their activity is stimulated by contact with target host cells. The sensing of target cells, thought to be mediated by the distal tip of the needle filament, generates an activating signal that must be transduced to the secretion machine by the needle filament. Here, through a multidisciplinary approach, including solid-state NMR (SSNMR) and cryo electron microscopy (cryo-EM) analyses, we have identified critical residues of the needle filament protein of a Salmonella Typhimurium type III secretion system that are involved in the regulation of the activity of the secretion machine. We found that mutations in the needle filament protein result in various specific phenotypes associated with different steps in the type III secretion process. More specifically, these studies reveal an important role for a polymorphic helix of the needle filament protein and the residues that line the lumen of its central channel in the control of type III secretion.
|Validation Report||PDB-ID: 6ofh|
SummaryFull reportAbout validation report
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_20046.map.gz / Format: CCP4 / Size: 3.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.708 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire filament structure of PrgI needle attached to the base
|Entire||Name: filament structure of PrgI needle attached to the base|
Number of components: 2
-Component #1: protein, filament structure of PrgI needle attached to the base
|Protein||Name: filament structure of PrgI needle attached to the base|
Recombinant expression: No
|Source||Species: Salmonella typhimurium (strain SL1344) (bacteria)|
-Component #2: protein, Protein PrgI
|Protein||Name: Protein PrgI / Number of Copies: 19 / Recombinant expression: No|
|Mass||Theoretical: 8.864868 kDa|
|Source||Species: Salmonella typhimurium (strain SL1344) (bacteria) / Strain: SL1344|
|Specimen||Specimen state: Filament / Method: cryo EM|
|Helical parameters||Axial symmetry: C1 (asymmetric) / Delta z: 4.24 Å / Delta phi: 63.35 %deg;|
|Sample solution||pH: 7.5|
|Vitrification||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: 47 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
|Processing||Method: helical reconstruction|
|3D reconstruction||Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF|
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