5TCQ

Near-atomic resolution cryo-EM structure of the Salmonella SPI-1 type III secretion injectisome secretin InvG

Summary for 5TCQ

• Entry DOI: 10.2210/pdb5tcq/pdb
• Related: 5TCP 5TCR
• EMDB information: 8398 8399 8400 8401
• Descriptor: Protein InvG (1 entity in total)
• Functional Keywords: bacterial, secretion, injectisome, membrane protein
• Biological source: Salmonella enterica subsp. enterica serovar Typhimurium
• Total number of polymer chains: 15
• Total formula weight: 927533.39

Authors

Worrall, L.J.,Hong, C.,Vuckovic, M.,Bergeron, J.R.C.,Huang, R.K.,Yu, Z.,Strynadka, N.C.J. (deposition date: 2016-09-15, release date: 2016-12-21, Last modification date: 2024-03-13)

Primary citation

Worrall, L.J.,Hong, C.,Vuckovic, M.,Deng, W.,Bergeron, J.R.,Majewski, D.D.,Huang, R.K.,Spreter, T.,Finlay, B.B.,Yu, Z.,Strynadka, N.C.
Near-atomic-resolution cryo-EM analysis of the Salmonella T3S injectisome basal body.
Nature, 540:597-601, 2016

PubMed Abstract: The type III secretion (T3S) injectisome is a specialized protein nanomachine that is critical for the pathogenicity of many Gram-negative bacteria, including purveyors of plague, typhoid fever, whooping cough, sexually transmitted infections and major nosocomial infections. This syringe-shaped 3.5-MDa macromolecular assembly spans both bacterial membranes and that of the infected host cell. The internal channel formed by the injectisome allows for the direct delivery of partially unfolded virulence effectors into the host cytoplasm. The structural foundation of the injectisome is the basal body, a molecular lock-nut structure composed predominantly of three proteins that form highly oligomerized concentric rings spanning the inner and outer membranes. Here we present the structure of the prototypical Salmonella enterica serovar Typhimurium pathogenicity island 1 basal body, determined using single-particle cryo-electron microscopy, with the inner-membrane-ring and outer-membrane-ring oligomers defined at 4.3 Å and 3.6 Å resolution, respectively. This work presents the first, to our knowledge, high-resolution structural characterization of the major components of the basal body in the assembled state, including that of the widespread class of outer-membrane portals known as secretins.

PubMed: 27974800
DOI: 10.1038/nature20576

Experimental method

ELECTRON MICROSCOPY (3.6 Å)