Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Near-atomic-resolution cryo-EM analysis of the Salmonella T3S injectisome basal body.
Journal, issue, pages	Nature, Vol. 540, Issue 7634, Page 597-601, Year 2016
Publish date	Dec 22, 2016
Authors	L J Worrall / C Hong / M Vuckovic / W Deng / J R C Bergeron / D D Majewski / R K Huang / T Spreter / B B Finlay / Z Yu / N C J Strynadka /
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, ...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.
External links	Nature / PubMed:27974800
Methods	EM (single particle)
Resolution	3.6 - 6.3 Å
Structure data	8398 5tcp EMDB-8398: Single particle cryo-EM reconstruction of the Salmonella SPI-1 type III secretion injectisome basal body at 4.3 Angstrom resolution PDB-5tcp: Near-atomic resolution cryo-EM structure of the periplasmic domains of PrgH and PrgK Method: EM (single particle) / Resolution: 4.3 Å 8399 5tcq EMDB-8399: Single particle cryo-EM reconstruction of the Salmonella SPI-1 type III secretion injectisome secretin InvG at 3.6 Angstrom resolution PDB-5tcq: Near-atomic resolution cryo-EM structure of the Salmonella SPI-1 type III secretion injectisome secretin InvG Method: EM (single particle) / Resolution: 3.6 Å 8400 5tcr EMDB-8400: 6.3 Angstrom structure of the Salmonella SPI-1 type III secretion injectisome basal body PDB-5tcr: Atomic model of the Salmonella SPI-1 type III secretion injectisome basal body proteins InvG, PrgH, and PrgK Method: EM (single particle) / Resolution: 6.3 Å EMDB-8401: Single particle cryo-EM reconstruction of the Salmonella SPI-1 type III secretion injectisome secretin InvG at 4.4 Angstrom resolution Method: EM (single particle) / Resolution: 4.4 Å
Source	salmonella enterica subsp. enterica serovar typhimurium (bacteria)
Keywords	MEMBRANE PROTEIN / Bacterial / secretion / injectisome