ArticleStructure (London, England : 1993)2013
The architecture of EssB, an integral membrane component of the type VII secretion system.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Crucial Gram-positive type IV secretion system protein TraF is a structural homolog of type VII secretion system protein EssB/YukC.microLife · 2026Article
- Protein Modeling with DEER Spectroscopy.Annual review of biophysics · 2025Review
- Article
- A novel approach to modeling side chain ensembles of the bifunctional spin label RX.bioRxiv : the preprint server for biology · 2023Article
- Article
- The Type VII Secretion System ofAnnual review of microbiology · 2021Article
- Type VII secretion systems: structure, functions and transport models.Nature reviews. Microbiology · 2021Review
- A membrane-depolarizing toxin substrate of theProceedings of the National Academy of Sciences of the United States of America · 2020Article
- The transmembrane domain of the Staphylococcus aureus ESAT-6 component EssB mediates interaction with the integral membrane protein EsaA, facilitating partially regulated secretion in a heterologous host.Archives of microbiology · 2018Article
- Isolation of a Membrane Protein Complex for Type VII Secretion in Staphylococcus aureus.Journal of bacteriology · 2017Article
- Flotillin scaffold activity contributes to type VII secretion system assembly in Staphylococcus aureus.PLoS pathogens · 2017Article
- EssC: domain structures inform on the elusive translocation channel in the Type VII secretion system.The Biochemical journal · 2016Article
- Membrane interactions and self-association of components of the Ess/Type VII secretion system of Staphylococcus aureus.FEBS letters · 2016Article
- Heterogeneity in ess transcriptional organization and variable contribution of the Ess/Type VII protein secretion system to virulence across closely related Staphylocccus aureus strains.Molecular microbiology · 2014Article
- mtsslSuite:Molecular physics · 2013Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The membrane-bound EssB is an integral and essential component of the bacterial type VII secretion system that can contribute to pathogenicity. The architecture of Geobacillus thermodenitrificans EssB has been investigated by combining crystallographic and EPR spectroscopic methods. The protein forms a dimer that straddles the cytoplasmic membrane. A helical fold is observed for the C-terminal segment, which is positioned on the exterior of the membrane. This segment contributes most to dimer formation. The N-terminal segment displays a structure related to the pseudokinase fold and may contribute to function by recognizing substrates or secretion system partners. The remaining part of EssB may serve as an anchor point for the secretion apparatus, which is embedded in the cytoplasmic membrane with the C-terminal domain protruding out to interact with partner proteins or components of peptidoglycan.
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Registered trials
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