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	T3S injectisome needle complex structures in four distinct states reveal the basis of membrane coupling and assembly.
Journal, issue, pages	Nat Microbiol, Vol. 4, Issue 11, Page 2010-2019, Year 2019
Publish date	Aug 19, 2019
Authors	Jinhong Hu / Liam J Worrall / Marija Vuckovic / Chuan Hong / Wanyin Deng / Claire E Atkinson / B Brett Finlay / Zhiheng Yu / Natalie C J Strynadka /
PubMed Abstract	The bacterial injectisome is a syringe-shaped macromolecular nanomachine utilized by many pathogenic Gram-negative bacteria, including the causative agents of plague, typhoid fever, whooping cough, ...The bacterial injectisome is a syringe-shaped macromolecular nanomachine utilized by many pathogenic Gram-negative bacteria, including the causative agents of plague, typhoid fever, whooping cough, sexually transmitted infections and major nosocomial infections. Bacterial proteins destined for self-assembly and host-cell targeting are translocated by the injectisome in a process known as type III secretion (T3S). The core structure is the ~4 MDa needle complex (NC), built on a foundation of three highly oligomerized ring-forming proteins that create a hollow scaffold spanning the bacterial inner membrane (IM) (24-mer ring-forming proteins PrgH and PrgK in the Salmonella enterica serovar Typhimurium Salmonella pathogenicity island 1 (SPI-1) type III secretion system (T3SS)) and outer membrane (OM) (15-mer InvG, a member of the broadly conserved secretin pore family). An internalized helical needle projects from the NC and bacterium, ultimately forming a continuous passage to the host, for delivery of virulence effectors. Here, we have captured snapshots of the entire prototypical SPI-1 NC in four distinct needle assembly states, including near-atomic resolution, and local reconstructions in the absence and presence of the needle. These structures reveal the precise localization and molecular interactions of the internalized SpaPQR 'export apparatus' complex, which is intimately encapsulated and stabilized within the IM rings in the manner of a nanodisc, and to which the PrgJ rod directly binds and functions as an initiator and anchor of needle polymerization. We also describe the molecular details of the extensive and continuous coupling interface between the OM secretin and IM rings, which is remarkably facilitated by a localized 16-mer stoichiometry in the periplasmic-most coupling domain of the otherwise 15-mer InvG oligomer.
External links	Nat Microbiol / PubMed:31427728
Methods	EM (single particle)
Resolution	3.42 - 6.0 Å
Structure data	20310 6q14 EMDB-20310: Salmonella SPI-1 injectisome NC-base class 1 PDB-6q14: Structure of the Salmonella SPI-1 injectisome NC-base Method: EM (single particle) / Resolution: 3.8 Å EMDB-20311: Salmonella SPI-1 injectisome NC-base class 2 Method: EM (single particle) / Resolution: 3.9 Å 20312 6q15 EMDB-20312: Salmonella SPI-1 injectisome needle complex with assembled needle PDB-6q15: Structure of the Salmonella SPI-1 injectisome needle complex Method: EM (single particle) / Resolution: 5.15 Å EMDB-20313: Salmonella SPI-1 injectisome needle complex with a trapped needle and the InvG secretin periplasmic gate in a partially unlocked state Method: EM (single particle) / Resolution: 4.75 Å EMDB-20314: Salmonella SPI-1 injectisome needle complex with a trapped needle and the InvG secretin periplasmic gate in an unlocked state Method: EM (single particle) / Resolution: 6.0 Å 20315 6pee EMDB-20315, PDB-6pee: InvG secretin domain beta-barrel from Salmonella SPI-1 injectisome NC-base Method: EM (single particle) / Resolution: 3.42 Å 20316 6pem EMDB-20316, PDB-6pem: Focussed refinement of InvGN0N1:SpaPQR:PrgHK from Salmonella SPI-1 injectisome NC-base Method: EM (single particle) / Resolution: 3.5 Å 20317 6pep EMDB-20317, PDB-6pep: Focussed refinement of InvGN0N1:SpaPQR:PrgIJ from the Salmonella SPI-1 injectisome needle complex Method: EM (single particle) / Resolution: 3.8 Å 20556 6q16 EMDB-20556, PDB-6q16: Focussed refinement of InvGN0N1:PrgHK:SpaPQR:PrgIJ from Salmonella SPI-1 injectisome NC-base Method: EM (single particle) / Resolution: 4.1 Å
Chemicals	ChemComp-LDA: LAURYL DIMETHYLAMINE-N-OXIDE / LDAO, detergent*YM / Lauryldimethylamine oxide
Source	Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344 (bacteria) salmonella typhimurium (strain lt2 / sgsc1412 / atcc 700720) (bacteria)
Keywords	PROTEIN TRANSPORT / Bacterial secretion / type III secretion / outer membrane / secretin / type III secretion system