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	A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion.
Journal, issue, pages	PLoS Biol, Vol. 17, Issue 7, Page e3000351, Year 2019
Publish date	Jul 1, 2019
Authors	Emily Z Guo / Daniel C Desrosiers / Jan Zalesak / James Tolchard / Mélanie Berbon / Birgit Habenstein / Thomas Marlovits / Antoine Loquet / Jorge E Galán /
PubMed Abstract	Type III protein-secretion machines are essential for the interactions of many pathogenic or symbiotic bacterial species with their respective eukaryotic hosts. The core component of these machines ...Type III protein-secretion machines are essential for the interactions of many pathogenic or symbiotic bacterial species with their respective eukaryotic hosts. The core component of these machines is the injectisome, a multiprotein complex that mediates the selection of substrates, their passage through the bacterial envelope, and ultimately their delivery into eukaryotic target cells. The injectisome is composed of a large cytoplasmic complex or sorting platform, a multiring base embedded in the bacterial envelope, and a needle-like filament that protrudes several nanometers from the bacterial surface and is capped at its distal end by the tip complex. A characteristic feature of these machines is that their activity is stimulated by contact with target host cells. The sensing of target cells, thought to be mediated by the distal tip of the needle filament, generates an activating signal that must be transduced to the secretion machine by the needle filament. Here, through a multidisciplinary approach, including solid-state NMR (SSNMR) and cryo electron microscopy (cryo-EM) analyses, we have identified critical residues of the needle filament protein of a Salmonella Typhimurium type III secretion system that are involved in the regulation of the activity of the secretion machine. We found that mutations in the needle filament protein result in various specific phenotypes associated with different steps in the type III secretion process. More specifically, these studies reveal an important role for a polymorphic helix of the needle filament protein and the residues that line the lumen of its central channel in the control of type III secretion.
External links	PLoS Biol / PubMed:31260457 / PubMed Central
Methods	EM (helical sym.)
Resolution	2.9 - 3.7 Å
Structure data	20043 6ofe EMDB-20043, PDB-6ofe: Helical reconstruction of Type III Secretion System Needle filament mutant-PrgI S49A Method: EM (helical sym.) / Resolution: 3.61 Å 20044 6off EMDB-20044, PDB-6off: High-resolution filamentous structures of in vitro polymerized PrgI needle Method: EM (helical sym.) / Resolution: 3.2 Å 20045 6ofg EMDB-20045, PDB-6ofg: In vitro polymerized PrgI V67A filaments Method: EM (helical sym.) / Resolution: 2.9 Å 20046 6ofh EMDB-20046, PDB-6ofh: Structure of Salmonella type III secretion system needle filament Method: EM (helical sym.) / Resolution: 3.7 Å
Source	salmonella typhimurium (strain sl1344) (bacteria) Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 (bacteria)
Keywords	PROTEIN TRANSPORT / Type III secretion / helical reconstruction / PrgI filament / salmonella / Type III secretion system