ArticleJournal of structural biology2013
Understanding specificity of the mycosin proteases in ESX/type VII secretion by structural and functional analysis.
Article in Journal of structural biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
20 citing papers in PubMed, 39 citations in OpenAlex.
- Sec and Tat Mediated Secretion Safeguards Mycobacterium tuberculosis Membrane Homeostasis.Molecular & cellular proteomics : MCP · 2026Article
- Article
- Disulfide bonds are required for cell division, cell envelope biogenesis and antibiotic resistance proteins in mycobacteria.bioRxiv : the preprint server for biology · 2025Article
- Structural Catalytic Core in Subtilisin-like Proteins and Its Comparison to Trypsin-like Serine Proteases and Alpha/Beta-Hydrolases.International journal of molecular sciences · 2024Review
- The Type VII Secretion System ofAnnual review of microbiology · 2021Article
- Recent Insights into the Structure and Function of Mycobacterial Membrane Proteins Facilitated by Cryo-EM.The Journal of membrane biology · 2021Review
- Modeling Tubercular ESX-1 Secretion Using Mycobacterium marinum.Microbiology and molecular biology reviews : MMBR · 2020Review
- High resolution CryoEM structure of the ring-shaped virulence factor EspB fromJournal of structural biology: X · 2020Article
- 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
- Esx Systems and the Mycobacterial Cell Envelope: What's the Connection?Journal of bacteriology · 2017Review
- Mycosins of the Mycobacterial Type VII ESX Secretion System: the Glue That Holds the Party Together.mBio · 2016Article
- Article
- Expression and production of solubleBiochemistry and biophysics reports · 2016Article
- Structure of EspB, a secreted substrate of the ESX-1 secretion system of Mycobacterium tuberculosis.Journal of structural biology · 2015Article
- Application of the 4D fingerprint method with a robust scoring function for scaffold-hopping and drug repurposing strategies.Journal of chemical information and modeling · 2014Article
- Pentapeptide boronic acid inhibitors of Mycobacterium tuberculosis MycP1 protease.Bioorganic & medicinal chemistry letters · 2014Article
- Article
- Novel mycosin protease MycP₁ inhibitors identified by virtual screening and 4D fingerprints.Journal of chemical information and modeling · 2014Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Mycobacteria use specialized ESX secretion systems to transport proteins across their cell membranes in order to manipulate their environment. In pathogenic Mycobacterium tuberculosis there are five paralogous ESX secretion systems, named ESX-1 through ESX-5. Each system includes a subtilisin-like protease (mycosin or MycP) as a core component essential for secretion. Here we report crystal structures of MycP1 and MycP3, the mycosins expressed by the ESX-1 and ESX-3 systems, respectively. In both mycosins the putative propeptide wraps around the catalytic domain and does not occlude the active site. The extensive contacts between the putative propeptide and catalytic domain, which include a disulfide bond, suggest that the N-terminal extension is an integral part of the active mycosin. The catalytic residues of MycP1 and MycP3 are located in a deep active site groove in contrast with an exposed active site in majority of subtilisins. We show that MycP1 specifically cleaves ESX-1 secretion-associated protein B (EspB) in vitro at residues Ala358 and Ala386. We also systematically characterize the specificity of MycP1 using peptide libraries, and show that it has evolved a narrow specificity relative to other subtilisins. Finally, comparison of the MycP1 and MycP3 structures suggest that both enzymes have stringent and different specificity profiles that result from the structurally distinct active site pockets, which could explain the system specific functioning of these proteases.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.