ArticleProtein science : a publication of the Protein Society2010
The crystal structure of the Mycobacterium tuberculosis Rv3019c-Rv3020c ESX complex reveals a domain-swapped heterotetramer.
Article in Protein science : a publication of the Protein Society, 2010. 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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20 citing papers in PubMed, 33 citations in OpenAlex.
- Genome-wide identification and characterization of the PE/PPE gene family in Mycobacterium abscessus.Functional & integrative genomics · 2026Article
- Protein-Mediated Virulence in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Differential expression of theApplied and environmental microbiology · 2024Article
- Mycobacterium tuberculosis and its clever approaches to escape the deadly macrophage.World journal of microbiology & biotechnology · 2023Review
- Multiple genetic paths including massive gene amplification allowProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Protein Export into and across the Atypical Diderm Cell Envelope of Mycobacteria.Microbiology spectrum · 2019Review
- Bacterial secretion chaperones: the mycobacterial type VII case.FEMS microbiology letters · 2018Review
- Isolation of a Membrane Protein Complex for Type VII Secretion in Staphylococcus aureus.Journal of bacteriology · 2017Article
- Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery.Molecules (Basel, Switzerland) · 2017Review
- Formation and carbon monoxide-dependent dissociation of Allochromatium vinosum cytochrome c' oligomers using domain-swapped dimers.Protein science : a publication of the Protein Society · 2017Article
- Structure of the methanofuran/methanopterin-biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Structure of the Mycobacterium tuberculosis type VII secretion system chaperone EspG5 in complex with PE25-PPE41 dimer.Molecular microbiology · 2014Article
- Dimer recognition and secretion by the ESX secretion system in Bacillus subtilis.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Comparative genomic and proteomic anatomy of Mycobacterium ubiquitous Esx family proteins: implications in pathogenicity and virulence.Current microbiology · 2014Article
- Secretion of atypical protein substrates by the ESAT-6 secretion system of Staphylococcus aureus.Molecular microbiology · 2013Article
- Article
- A β-Lactamase based reporter system for ESX dependent protein translocation in mycobacteria.PloS one · 2012Article
- Comparative genomics of Esx genes from clinical isolates of Mycobacterium tuberculosis provides evidence for gene conversion and epitope variation.Infection and immunity · 2011Article
- Solution structure of the Mycobacterium tuberculosis EsxG·EsxH complex: functional implications and comparisons with other M. tuberculosis Esx family complexes.The Journal of biological chemistry · 2011Article
- The homodimeric GBS1074 from Streptococcus agalactiae.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
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6 authors at 1 institution in 1 country.
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Abstract
Mycobacterium tuberculosis encodes five gene clusters (ESX-1 to ESX-5) for Type VII protein secretion systems that are implicated in mycobacterial pathogenicity. Substrates for the secretion apparatus are encoded within the gene clusters and in additional loci that lack the components of the secretion apparatus. The best characterized substrates are the ESX complexes, 1:1 heterodimers of ESAT-6 and CFP-10, the prototypical member that has been shown to be essential for Mycobacterium tuberculosis pathogenesis. We have determined the structure of EsxRS, a homolog of EsxGH of the ESX-3 gene cluster, at 1.91 Å resolution. The EsxRS structure is composed of two four-helix bundles resulting from the 3D domain swapping of the C-terminal domain of EsxS, the CFP-10 homolog. The four-helix bundles at the extremities of the complex have a similar architecture to the structure of ESAT-6·CFP-10 (EsxAB) of ESX-1, but in EsxRS a hinge loop linking the α-helical domains of EsxS undergoes a loop-to-helix transition that creates the domain swapped EsxRS tetramer. Based on the atomic structure of EsxRS and existing biochemical data on ESX complexes, we propose that higher order ESX oligomers may increase avidity of ESX binding to host receptor molecules or, alternatively, the conformational change that creates the domain swapped structure may be the basis of ESX complex dissociation that would free ESAT-6 to exert a cytotoxic effect.
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