ArticleBMC structural biology2016
Structures of EccB1 and EccD1 from the core complex of the mycobacterial ESX-1 type VII secretion system.
Article in BMC structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 36 citations in OpenAlex.
- Article
- Sec and Tat Mediated Secretion Safeguards Mycobacterium tuberculosis Membrane Homeostasis.Molecular & cellular proteomics : MCP · 2026Article
- Genome-wide phenotypic insights into mycobacterial virulence using Drosophila melanogaster.PLoS pathogens · 2025Article
- Whole-genome sequencing analysis to identify antimicrobial resistance regions and virulence factors in Mycobacterium tuberculosis isolates from the Amhara Region, Ethiopia.Scientific reports · 2025Article
- Assembly of a unique membrane complex in type VI secretion systems of Bacteroidota.Nature communications · 2024Article
- Type VII secretion systems: structure, functions and transport models.Nature reviews. Microbiology · 2021Review
- Structure of the mycobacterial ESX-5 type VII secretion system pore complex.Science advances · 2021Article
- Modeling Tubercular ESX-1 Secretion Using Mycobacterium marinum.Microbiology and molecular biology reviews : MMBR · 2020Review
- Mycobacterial Virulence Factors: Surface-Exposed Lipids and Secreted Proteins.International journal of molecular sciences · 2020Review
- Article
- Article
- Protein Export into and across the Atypical Diderm Cell Envelope of Mycobacteria.Microbiology spectrum · 2019Review
- Protease domain and transmembrane domain of the type VII secretion mycosin protease determine system-specific functioning in mycobacteria.The Journal of biological chemistry · 2019Article
- Functional analysis of the EsaB component of theMicrobiology (Reading, England) · 2017Article
- Esx Systems and the Mycobacterial Cell Envelope: What's the Connection?Journal of bacteriology · 2017Review
- Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundThe ESX-1 type VII secretion system is an important determinant of virulence in pathogenic mycobacteria, including Mycobacterium tuberculosis. This complicated molecular machine secretes folded proteins through the mycobacterial cell envelope to subvert the host immune response. Despite its important role in disease very little is known about the molecular architecture of the ESX-1 secretion system.
resultsThis study characterizes the structures of the soluble domains of two conserved core ESX-1 components - EccB1 and EccD1. The periplasmic domain of EccB1 consists of 4 repeat domains and a central domain, which together form a quasi 2-fold symmetrical structure. The repeat domains of EccB1 are structurally similar to a known peptidoglycan binding protein suggesting a role in anchoring the ESX-1 system within the periplasmic space. The cytoplasmic domain of EccD1has a ubiquitin-like fold and forms a dimer with a negatively charged groove.
conclusionsThese structures represent a major step towards resolving the molecular architecture of the entire ESX-1 assembly and may contribute to ESX-1 targeted tuberculosis intervention strategies.
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