6DV6

Structure of the Salmonella SPI-1 type III secretion injectisome secretin InvG (residues 176-end) in the open gate state

Summary for 6DV6

• Entry DOI: 10.2210/pdb6dv6/pdb
• EMDB information: 8913 8914 8915
• Descriptor: Protein InvG (1 entity in total)
• Functional Keywords: type iii secretion system, secretin, membrane protein
• Biological source: Salmonella enterica subsp. enterica serovar Typhimurium
• Total number of polymer chains: 15
• Total formula weight: 927533.39

Authors

Hu, J.,Worrall, L.J.,Vuckovic, M.,Atkinson, C.E.,Strynadka, N.C.J. (deposition date: 2018-06-22, release date: 2018-10-03, Last modification date: 2024-03-13)

Primary citation

Hu, J.,Worrall, L.J.,Hong, C.,Vuckovic, M.,Atkinson, C.E.,Caveney, N.,Yu, Z.,Strynadka, N.C.J.
Cryo-EM analysis of the T3S injectisome reveals the structure of the needle and open secretin.
Nat Commun, 9:3840-3840, 2018

PubMed Abstract: 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 from the prototypical Salmonella Typhimurium SPI-1 type III secretion system, with local masking protocols allowing for model building and refinement of the major membrane spanning components of the needle complex base in addition to an isolated needle filament. This work provides significant insight into injectisome structure and assembly and importantly captures the molecular basis for substrate induced gating in the giant outer membrane secretin portal family.

PubMed: 30242280
DOI: 10.1038/s41467-018-06298-8

Experimental method

ELECTRON MICROSCOPY (3.9 Å)