ArticleJournal of molecular biology2008
Structures of the Shigella flexneri type 3 secretion system protein MxiC reveal conformational variability amongst homologues.
Article in Journal of molecular biology, 2008. 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.
- Oligomeric assembly of the gatekeeper InvE orchestrates hierarchical type III protein secretion inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Calcium controls type III secretion switch through an SctV-SctW interplay.Frontiers in microbiology · 2026Article
- BopN is a Gatekeeper of theMicrobiology spectrum · 2023Article
- Staying out or Going in? The Interplay between Type 3 and Type 5 Secretion Systems in Adhesion and Invasion of Enterobacterial Pathogens.International journal of molecular sciences · 2020Review
- The inner-rod component of Shigella flexneri type 3 secretion system, MxiI, is involved in the transmission of the secretion activation signal by its interaction with MxiC.MicrobiologyOpen · 2018Article
- Steps for Shigella Gatekeeper Protein MxiC Function in Hierarchical Type III Secretion Regulation.The Journal of biological chemistry · 2017Article
- The Structure and Function of Type III Secretion Systems.Microbiology spectrum · 2016Review
- Type Three Secretion System in Attaching and Effacing Pathogens.Frontiers in cellular and infection microbiology · 2016Review
- MxiA, MxiC and IpaD Regulate Substrate Selection and Secretion Mode in the T3SS of Shigella flexneri.PloS one · 2016Article
- Type III secretion systems: the bacterial flagellum and the injectisome.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- Structural analysis of SepL, an enteropathogenic Escherichia coli type III secretion-system gatekeeper protein.Acta crystallographica. Section F, Structural biology communications · 2015Article
- A gatekeeper chaperone complex directs translocator secretion during type three secretion.PLoS pathogens · 2014Article
- Biochemical and structural insights into microtubule perturbation by CopN from Chlamydia pneumoniae.The Journal of biological chemistry · 2014Article
- Control of type III secretion activity and substrate specificity by the cytoplasmic regulator PcrG.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- 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
- The Chlamydia effector chlamydial outer protein N (CopN) sequesters tubulin and prevents microtubule assembly.The Journal of biological chemistry · 2011Article
- The Shigella T3SS needle transmits a signal for MxiC release, which controls secretion of effectors.Molecular microbiology · 2010Article
- Salmonella pathogenesis and processing of secreted effectors by caspase-3.Science (New York, N.Y.) · 2010Article
- Timing is everything: the regulation of type III secretion.Cellular and molecular life sciences : CMLS · 2010Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Many Gram-negative pathogenic bacteria use a complex macromolecular machine, known as the type 3 secretion system (T3SS), to transfer virulence proteins into host cells. The T3SS is composed of a cytoplasmic bulb, a basal body spanning the inner and outer bacterial membranes, and an extracellular needle. Secretion is regulated by both cytoplasmic and inner membrane proteins that must respond to specific signals in order to ensure that virulence proteins are not secreted before contact with a eukaryotic cell. This negative regulation is mediated, in part, by a family of proteins that are thought to physically block the entrance to the secretion apparatus until an appropriate signal is received following host cell contact. Despite weak sequence homology between proteins of this family, the crystal structures of Shigella flexneri MxiC we present here confirm the conservation of domain topology with the homologue from Yersinia sp. Interestingly, comparison of the Shigella and Yersinia structures reveals a significant structural change that results in substantial domain re-arrangement and opening of one face of the molecule. The conservation of a negatively charged patch on this face suggests it may have a role in binding other components of the T3SS.
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