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	High-resolution view of the type III secretion export apparatus in situ reveals membrane remodeling and a secretion pathway.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 116, Issue 49, Page 24786-24795, Year 2019
Publish date	Dec 3, 2019
Authors	Carmen Butan / Maria Lara-Tejero / Wenwei Li / Jun Liu / Jorge E Galán /
PubMed Abstract	Type III protein secretion systems are essential virulence factors for many important pathogenic bacteria. The entire protein secretion machine is composed of several substructures that organize into ...Type III protein secretion systems are essential virulence factors for many important pathogenic bacteria. The entire protein secretion machine is composed of several substructures that organize into a holostructure or injectisome. The core component of the injectisome is the needle complex, which houses the export apparatus that serves as a gate for the passage of the secreted proteins through the bacterial inner membrane. Here, we describe a high-resolution structure of the export apparatus of the type III secretion system in association with the needle complex and the underlying bacterial membrane, both in isolation and in situ. We show the precise location of the core export apparatus components within the injectisome and bacterial envelope and demonstrate that their deployment results in major membrane remodeling and thinning, which may be central for the protein translocation process. We also show that InvA, a critical export apparatus component, forms a multiring cytoplasmic conduit that provides a pathway for the type III secretion substrates to reach the entrance of the export gate. Combined with structure-guided mutagenesis, our studies provide major insight into potential mechanisms of protein translocation and injectisome assembly.
External links	Proc Natl Acad Sci U S A / PubMed:31744874 / PubMed Central
Methods	EM (single particle) / EM (subtomogram averaging)
Resolution	3.3 - 17.0 Å
Structure data	EMDB-20830: Cryo-EM reconstruction of the inner membrane rings containing the core components of the export apparatus and associated membranes of the needle complex from Salmonella typhimurium type III secretion system. Method: EM (single particle) / Resolution: 3.93 Å EMDB-20831: Cryo-EM reconstruction shows that the needle complex's inner rings from Salmonella assemble with 23-fold symmetry in the absence of the export apparatus. Method: EM (single particle) / Resolution: 5.3 Å 20832 6uot EMDB-20832, PDB-6uot: Cryo-EM structure of the PrgHK periplasmic ring from the Salmonella SPI-1 type III secretion needle complex solved at 3.3 angstrom resolution Method: EM (single particle) / Resolution: 3.3 Å 20833 6uov EMDB-20833, PDB-6uov: Cryo-EM reconstruction of the PrgHK periplasmic ring from Salmonella's needle complex assembled in the absence of the export apparatus Method: EM (single particle) / Resolution: 3.5 Å EMDB-20838: In situ structure of the export apparatus in Salmonella T3SS machine Method: EM (subtomogram averaging) / Resolution: 17.0 Å
Source	salmonella enterica subsp. enterica serovar typhimurium (bacteria) Salmonella enterica subsp. enterica serovar Abony (bacteria)
Keywords	MEMBRANE PROTEIN / BACTERIAL NANOMACHINE / TYPE III SECRETION SYSTEM