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Crystal structure of the itYersinia enterocolitica/it type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD By Schreiner Madeleine and Niemann Hartmut H No static citation data No static citation data Cite
(A) Left: cryo-EM image of a Yersinia enterocolitica bacteria (left half of the panel) and a 20-nm thick slice through a tomogram of the bacteria showing an injectisome (right half of the panel black arrowhead) Right: volume rendering of the same Y enterocolitica bacteria showing the inner (yellow) and outer (blue) membranes and injectisomes (red)
2008-1-25Structure of the Yersinia enterocolitica Type III Secretion Translocator Chaperone SycD The crystal structure of SycD and the identification of a new interaction surface in the translocator chaperone contribute to the understanding of its versatile functionality Although both the convex as well as the concave side of the TPR in the SycD
The outer membrane (OM) of Gram-negative bacteria poses a barrier to antibiotic entry due to its high impermeability Thus there is an urgent need to study the function and biogenesis of the OM In Enterobacterales an order of bacteria with many pathogenic members one of the components of the OM is enterobacterial common antigen (ECA) We have known of the presence of ECA on the cell
LcrV a multifunctional protein acts as a positive regulator of effector protein secretion for the type III secretion system (T3SS) in Yersinia pestis by interaction with the negative regulator LcrG In this study LcrV was analyzed to identify regions required for LcrG interaction Random-linker insertion mutagenesis deletion analysis and site-directed mutagenesis of hydrophobic amino
2020-4-22The enteric pathogen Y enterocolitica uses a injection machinery called type III secretion system (T3SS) to translocate effector proteins across eukaryotic cell membranes The supramolecular structure of the T3SS is evolutionarily related to the bacterial flagellum
The delivery of virulence factors into host cells through type III secretion systems is essential for enterobacterial pathogenesis Molecular chaperones bind specifically to virulence factors in the bacterial cytosol before secretion Invasion plasmid gene C (IpgC) is a chaperone that binds 2 essential virulence factors of Shigella : invasion plasmid antigens (Ipa) B and C
2020-4-22The enteric pathogen Y enterocolitica uses a injection machinery called type III secretion system (T3SS) to translocate effector proteins across eukaryotic cell membranes The supramolecular structure of the T3SS is evolutionarily related to the bacterial flagellum
Pathogenic Yersinia species use a type III secretion system (TTSS) encoded by the virulence plasmid to inject a number of effector proteins (Y ersinia o uter p roteins abbrev Yops) into eucaryotic host cells [1–3] The complex transport machinery (also denoted as injectisome) consists of some 25 components A needle-like structure polymerized from YscF with a hollow center of about 2–3
Crystal structure of Yersinia enterocolitica type III secretion chaperone SycT Crystal structure of Yersinia enterocolitica type III secretion chaperone SycT Bttner Carina R Cornelis Guy R Heinz Dirk W Niemann Hartmut H 2005-08-01 00:00:00 Pathogenic Yersinia species use a type III secretion (TTS) system to deliver a number of cytotoxic effector proteins directly into the
(A) Left: cryo-EM image of a Yersinia enterocolitica bacteria (left half of the panel) and a 20-nm thick slice through a tomogram of the bacteria showing an injectisome (right half of the panel black arrowhead) Right: volume rendering of the same Y enterocolitica bacteria showing the inner (yellow) and outer (blue) membranes and injectisomes (red)
2008-1-25Structure of the Yersinia enterocolitica Type III Secretion Translocator Chaperone SycD The crystal structure of SycD and the identification of a new interaction surface in the translocator chaperone contribute to the understanding of its versatile functionality Although both the convex as well as the concave side of the TPR in the SycD
The type III secretion system machinery also known as the injectisome delivers bacterial effector proteins into eukaryotic cells during infection The outer membrane YscC secretin is a major part of Yersinia enterocolitica's injectisome and is among the first components to assemble solely assisted by its pilotin YscW We have determined
Pathogenic yersiniae (Y pestis Y pseudotuberculosis Y enterocolitica) share a virulence plasmid encoding a type three secretion system (T3SS) This T3SS comprises more than 40 constituents Among these are the transport substrates called Yops (Yersinia outer proteins) the specific Yop chaperones (Sycs) and the Ysc (Yop secretion) proteins which form the transport machinery
The type III secretion system machinery also known as the injectisome delivers bacterial effector proteins into eukaryotic cells during infection The outer membrane YscC secretin is a major part of Yersinia enterocolitica's injectisome and is among the first components to assemble solely assisted by its pilotin YscW We have determined
Here we report the crystal structure of the YscEFG protein complex at 1 8 {angstrom} resolution Overall the structure is similar to that of the analogous PscEFG complex from the Pseudomonas aeruginosa type III secretion system but there are noteworthy differences
2009-12-11in the genus Yersinia It has three different type III secretion systems Ysc Ysa and the flagella The effect of flagella on biofilm formation was evaluated In a panel of 31 mutant Y enterocolitica strains the mutations that abolish the structure or rotation of
2005-9-2Prior to secretion some of these effectors are accompanied by specific type III secretion chaperones The Yersinia enterocolitica TTSS chaperone SycT escorts the effector YopT a cysteine protease that inactivates the small GTPase RhoA of targeted host cells We solved the crystal structure of SycT at 2 5 resolution
2005-8-1Structure of Spa15 a type III secretion chaperone from Shigella flexneri with broad specificity EMBO Rep 5 477–483 [PMC free article] [Google Scholar] Wattiau P and Cornelis G R 1993 SycE a chaperone-like protein of Yersinia enterocolitica involved in the secretion of YopE Mol Microbiol 8 123–131 [Google Scholar]
2012-7-16Structure Review Biogenesis Regulation and Targeting of the Type III Secretion System ? ? Thierry Izore 1 2 3 Viviana Job 1 2 3 and Andrea Dessen1 2 3 * Pathogenesis Group a l'Energie Atomique 3Centre National de la Recherche Scienti?que ?
Yersinia enterocolitica biovar 1B is one of a number of strains pathogenic to humans in the genus Yersinia It has three different type III secretion systems Ysc Ysa and the flagella In this study the effect of flagella on biofilm formation was evaluated In a panel of 31 mutant Y enterocolitica strains we observed that mutations
The development of effective innate and subsequent adaptive host immune responses is highly dependent on the production of proinflammatory cytokines that increase the activity of immune cells The key role in this process is played by inflammasomes multimeric protein complexes serving as a platform for caspase-1 an enzyme responsible for proteolytic cleavage of IL-1i#x3b2 /i and IL-18
Pathogenic yersiniae (Y pestis Y pseudotuberculosis Y enterocolitica) share a virulence plasmid encoding a type three secretion system (T3SS) This T3SS comprises more than 40 constituents Among these are the transport substrates called Yops (Yersinia outer proteins) the specific Yop chaperones (Sycs) and the Ysc (Yop secretion) proteins which form the transport machinery
Pathogenic yersiniae (Y pestis Y pseudotuberculosis Y enterocolitica) share a virulence plasmid encoding a type three secretion system (T3SS) This T3SS comprises more than 40 constituents Among these are the transport substrates called Yops (Yersinia outer proteins) the specific Yop chaperones (Sycs) and the Ysc (Yop secretion) proteins which form the transport machinery
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