Dataset Information


Identification of proteins in the Salmonella SPI-1 type III secretion injectisome needle complex

ABSTRACT: We determined the cryo-EM structure of the type III secretion injectisome needle complex. We used LC-MS/MS to idensitfy the constituent proteins showing the predominant presence of the major inner- and outer basal body proteins (PrgH+PrgK and InvG respectively), export apparatus protein SpaP and SpaR, and the rod and needle filament proteins PrgJ and PrgI.


ORGANISM(S): Salmonella enterica subsp. enterica serovar Typhimurium str. LT2  

TISSUE(S): Tissue Not Applicable To Dataset

DISEASE(S): Not Available

SUBMITTER: Liam Worrall  

LAB HEAD: Natalie Strynadka

PROVIDER: PXD010239 | Pride | 2018-10-16


Dataset's files

Action DRS
analysis.baf Other
ceba4fee-0a00-4522-95d2-db0cd4dbc59d_1.mcf Other
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Cryo-EM analysis of the T3S injectisome reveals the structure of the needle and open secretin.

Hu J J   Worrall L J LJ   Hong C C   Vuckovic M M   Atkinson C E CE   Caveney N N   Yu Z Z   Strynadka N C J NCJ  

Nature communications 20180921 1

The bacterial type III secretion system, or injectisome, is a syringe shaped nanomachine essential for the virulence of many disease causing Gram-negative bacteria. At the core of the injectisome structure is the needle complex, a continuous channel formed by the highly oligomerized inner and outer membrane hollow rings and a polymerized helical needle filament which spans through and projects into the infected host cell. Here we present the near-atomic resolution structure of a needle complex f  ...[more]

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