ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
The homodimeric GBS1074 from Streptococcus agalactiae.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Type VIIb secretion systems in Lactobacillales: insights from streptococci and enterococci.Journal of bacteriology · 2026Review
- Differential expression of theApplied and environmental microbiology · 2024Article
- Interbacterial competition mediated by the type VIIb secretion system.Microbiology (Reading, England) · 2023Review
- A novel variant of theMicrobial genomics · 2023Article
- Protein Export into and across the Atypical Diderm Cell Envelope of Mycobacteria.Microbiology spectrum · 2019Review
- 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
- 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
- WXG100 protein superfamily consists of three subfamilies and exhibits an α-helical C-terminal conserved residue pattern.PloS one · 2014Article
- Secretion of atypical protein substrates by the ESAT-6 secretion system of Staphylococcus aureus.Molecular microbiology · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ESAT-6 is a well characterized secreted protein from Mycobacterium tuberculosis and represents the archetype of the WXG100 family of proteins. Genes encoding ESAT-6 homologues have been identified in the genome of the human pathogen Streptococcus agalactiae; one of these genes, esxA, has been cloned and the recombinant protein has been crystallized. In contrast to M. tuberculosis ESAT-6, the crystal structure of GBS1074 reveals a homodimeric structure similar to homologous structures from Staphylococcus aureus and Helicobacter pylori. Intriguingly, GBS1074 forms elongated fibre-like assemblies in the crystal structure.
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