ArticleThe Journal of biological chemistry2011
Characterization of the interaction between the Salmonella type III secretion system tip protein SipD and the needle protein PrgI by paramagnetic relaxation enhancement.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Concentration and time-dependent amyloidogenic characteristics of intrinsically disordered N-terminal region ofFrontiers in microbiology · 2023Article
- An antibody targeting type III secretion system induces broad protection against Salmonella and Shigella infections.PLoS neglected tropical diseases · 2021Article
- Type three secretion system in Salmonella Typhimurium: the key to infection.Genes & genomics · 2020Review
- The type III secretion system needle, tip, and translocon.Protein science : a publication of the Protein Society · 2019Review
- A B-Z junction induced by an A … A mismatch in GAC repeats in the gene for cartilage oligomeric matrix protein promotes binding with the hZαThe Journal of biological chemistry · 2017Article
- NMR insight into myosin-binding subunit coiled-coil structure reveals binding interface with protein kinase G-Iα leucine zipper in vascular function.The Journal of biological chemistry · 2017Article
- Article
- Macrophage Apoptosis Triggered by IpaD from Shigella flexneri.Infection and immunity · 2016Article
- Characterization of the Binding of Hydroxyindole, Indoleacetic acid, and Morpholinoaniline to the Salmonella Type III Secretion System Proteins SipD and SipB.ChemMedChem · 2016Article
- Characterization of the Shigella and Salmonella Type III Secretion System Tip-Translocon Protein-Protein Interaction by Paramagnetic Relaxation Enhancement.Chembiochem : a European journal of chemical biology · 2016Article
- The bacterial type III secretion system as a target for developing new antibiotics.Chemical biology & drug design · 2015Article
- NMR model of PrgI-SipD interaction and its implications in the needle-tip assembly of the Salmonella type III secretion system.Journal of molecular biology · 2014Article
- Bacterial type III secretion systems: specialized nanomachines for protein delivery into target cells.Annual review of microbiology · 2014Review
- An introduction to biological NMR spectroscopy.Molecular & cellular proteomics : MCP · 2013Review
- Structure of the Yersinia pestis tip protein LcrV refined to 1.65 Å resolution.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Structure and biophysics of type III secretion in bacteria.Biochemistry · 2013Review
- The common structural architecture of Shigella flexneri and Salmonella typhimurium type three secretion needles.PLoS pathogens · 2013Article
- Shigella IpaD has a dual role: signal transduction from the type III secretion system needle tip and intracellular secretion regulation.Molecular microbiology · 2013Article
- Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.Microbiology and molecular biology reviews : MMBR · 2012Review
- Crystal structure of PrgI-SipD: insight into a secretion competent state of the type three secretion system needle tip and its interaction with host ligands.PLoS pathogens · 2011Article
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3 authors.
Funding
Abstract
Many Gram-negative bacteria that cause major diseases and mortality worldwide require the type III secretion system (T3SS) to inject virulence proteins into their hosts and cause infections. A structural component of the T3SS is the needle apparatus, which consists of a base, an external needle, and a tip complex. In Salmonella typhimurium, the external needle is assembled by the polymerization of the needle protein PrgI. On top of this needle sits a tip complex, which is partly formed by the tip protein SipD. How SipD interacts with PrgI during the assembly of the T3SS needle apparatus remains unknown. The central region of PrgI forms an α-helical hairpin, whereas SipD has a long central coiled-coil, which is a defining structural feature of other T3SS tip proteins as well. Using NMR paramagnetic relaxation enhancement, we have identified a specific region on the SipD coiled-coil that interacts directly with PrgI. We present a model of how SipD might dock at the tip of the needle based on our paramagnetic relaxation enhancement results, thus offering new insight about the mechanism of assembly of the T3SS needle apparatus.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.