ArticleJournal of molecular biology2014
NMR model of PrgI-SipD interaction and its implications in the needle-tip assembly of the Salmonella type III secretion system.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Review
- Ultraweak interactions drive cap-mediated positioning and elongation of the bacterial flagellar filament.Nature communications · 2025Article
- Virulence-associated type III secretion systems in Gram-negative bacteria.Microbiology (Reading, England) · 2023Review
- Recent insights into type-3 secretion system injectisome structure and mechanism of human enteric pathogens.Current opinion in microbiology · 2023Review
- Manipulation of host immune defenses by effector proteins delivered from multiple secretion systems ofFrontiers in immunology · 2023Review
- Concentration and time-dependent amyloidogenic characteristics of intrinsically disordered N-terminal region ofFrontiers in microbiology · 2023Article
- Cryo-EM structure of the needle filament tip complex of theProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Type 3 secretion system 1 of Salmonella typhimurium and its inhibitors: a novel strategy to combat salmonellosis.Environmental science and pollution research international · 2021Review
- 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
- Review
- Integrative Protein Modeling in RosettaNMR from Sparse Paramagnetic Restraints.Structure (London, England : 1993) · 2019Article
- The type III secretion system needle, tip, and translocon.Protein science : a publication of the Protein Society · 2019Review
- A polymorphic helix of a Salmonella needle protein relays signals defining distinct steps in type III secretion.PLoS biology · 2019Article
- Visualization of the type III secretion mediatedeLife · 2018Article
- Bacterial type III secretion systems: a complex device for the delivery of bacterial effector proteins into eukaryotic host cells.FEMS microbiology letters · 2018Review
- 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
- Single-domain antibodies pinpoint potential targets withinThe Journal of biological chemistry · 2017Article
- Acylation of the Type 3 Secretion System Translocon Using a Dedicated Acyl Carrier Protein.PLoS genetics · 2017Article
- Article
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9 authors.
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Abstract
Salmonella and other pathogenic bacteria use the type III secretion system (T3SS) to inject virulence proteins into human cells to initiate infections. The structural component of the T3SS contains a needle and a needle tip. The needle is assembled from PrgI needle protomers and the needle tip is capped with several copies of the SipD tip protein. How a tip protein docks on the needle is unclear. A crystal structure of a PrgI-SipD fusion protein docked on the PrgI needle results in steric clash of SipD at the needle tip when modeled on the recent atomic structure of the needle. Thus, there is currently no good model of how SipD is docked on the PrgI needle tip. Previously, we showed by NMR paramagnetic relaxation enhancement (PRE) methods that a specific region in the SipD coiled coil is the binding site for PrgI. Others have hypothesized that a domain of the tip protein-the N-terminal α-helical hairpin-has to swing away during the assembly of the needle apparatus. Here, we show by PRE methods that a truncated form of SipD lacking the α-helical hairpin domain binds more tightly to PrgI. Further, PRE-based structure calculations revealed multiple PrgI binding sites on the SipD coiled coil. Our PRE results together with the recent NMR-derived atomic structure of the Salmonella needle suggest a possible model of how SipD might dock at the PrgI needle tip. SipD and PrgI are conserved in other bacterial T3SSs; thus, our results have wider implication in understanding other needle-tip complexes.
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