ArticleScience advances2021
Structure of the mycobacterial ESX-5 type VII secretion system pore complex.
Article in Science advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- EsxA is required for antibacterial toxin export by the type VIIb secretion system.The Journal of biological chemistry · 2026Article
- A Type VII-secreted toxin enables inter-mycobacterial competition.Nature communications · 2026Article
- ThemBio · 2026Article
- Sigma factor M induces an ESX-4-focused regulon inFrontiers in tuberculosis · 2026Article
- Evaluating selection at intermediate scales within genes provides robust identification of genes under positive selection in M. tuberculosis clinical isolates.Tuberculosis (Edinburgh, Scotland) · 2025Article
- Control of Mycobacterium tuberculosis protein secretion by ESX-4 and the outer membrane EsxUT-EsxEF complex.Nature communications · 2025Article
- Evaluating selection at intermediate scales within genes provides robust identification of genes under positive selection inbioRxiv : the preprint server for biology · 2025Article
- Frontiers in integrative structural modeling of macromolecular assemblies.QRB discovery · 2025Review
- Deep mutational scanning of EccDbioRxiv : the preprint server for biology · 2024Article
- High-throughput functional analysis provides novel insight into type VII secretion inOpen biology · 2024Article
- New insights into the domain of unknown function (DUF) of EccCActa crystallographica. Section D, Structural biology · 2024Article
- Impact of MSMEG5257 Deletion onMicroorganisms · 2024Article
- Proteomics from compartment-specific APEX2 labeling in Mycobacterium tuberculosis reveals Type VII secretion substrates in the cell wall.Cell chemical biology · 2024Article
- Assembly of a unique membrane complex in type VI secretion systems of Bacteroidota.Nature communications · 2024Article
- The role of proteinaceous toxins secreted byFEMS microbes · 2024Review
- Article
- A type VII-secreted lipase toxin with reverse domain arrangement.Nature communications · 2023Article
- Interbacterial competition mediated by the type VIIb secretion system.Microbiology (Reading, England) · 2023Review
- Article
- Novel Artificial Intelligence-Based Approaches for Ab Initio Structure Determination and Atomic Model Building for Cryo-Electron Microscopy.Micromachines · 2023Review
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ESX-5 type VII secretion system is a membrane-spanning protein complex key to the virulence of mycobacterial pathogens. However, the overall architecture of the fully assembled translocation machinery and the composition of the central secretion pore have remained unknown. Here, we present the high-resolution structure of the 2.1-megadalton ESX-5 core complex. Our structure captured a dynamic, secretion-competent conformation of the pore within a well-defined transmembrane section, sandwiched between two flexible protein layers at the cytosolic entrance and the periplasmic exit. We propose that this flexibility endows the ESX-5 machinery with large conformational plasticity required to accommodate targeted protein secretion. Compared to known secretion systems, a highly dynamic state of the pore may represent a fundamental principle of bacterial secretion machineries.
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Registered trials
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