ArticleThe Journal of biological chemistry2011
Oligomerization of EpsE coordinates residues from multiple subunits to facilitate ATPase activity.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 33 citations in OpenAlex.
- Old role with new feature: T2SS ATPase as a cyclic-di-GMP receptor to regulate antibiotic production.Applied and environmental microbiology · 2024Article
- Membrane platform protein PulF of themBio · 2024Article
- Article
- Structure and Membrane Topography of the Vibrio-Type Secretin Complex from the Type 2 Secretion System of Enteropathogenic Escherichia coli.Journal of bacteriology · 2018Article
- Zinc coordination is essential for the function and activity of the type II secretion ATPase EpsE.MicrobiologyOpen · 2016Article
- Systematic Identification of Cyclic-di-GMP Binding Proteins in Vibrio cholerae Reveals a Novel Class of Cyclic-di-GMP-Binding ATPases Associated with Type II Secretion Systems.PLoS pathogens · 2015Article
- Editorial.FEMS microbiology reviews · 2015Article
- Exceptionally widespread nanomachines composed of type IV pilins: the prokaryotic Swiss Army knives.FEMS microbiology reviews · 2015Review
- Crystal structure of the full-length ATPase GspE from the Vibrio vulnificus type II secretion system in complex with the cytoplasmic domain of GspL.Journal of structural biology · 2014Article
- Distinct docking and stabilization steps of the Pseudopilus conformational transition path suggest rotational assembly of type IV pilus-like fibers.Structure (London, England : 1993) · 2014Article
- Hexamers of the type II secretion ATPase GspE from Vibrio cholerae with increased ATPase activity.Structure (London, England : 1993) · 2013Article
- Cysteine scanning mutagenesis and disulfide mapping analysis of arrangement of GspC and GspD protomers within the type 2 secretion system.The Journal of biological chemistry · 2012Article
- On the path to uncover the bacterial type II secretion system.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- The type II secretion system: biogenesis, molecular architecture and mechanism.Nature reviews. Microbiology · 2012Review
- Structural insights into the Type II secretion nanomachine.Current opinion in structural biology · 2012Review
- Deciphering the Xcp Pseudomonas aeruginosa type II secretion machinery through multiple interactions with substrates.The Journal of biological chemistry · 2011Article
- Structural and functional studies on the interaction of GspC and GspD in the type II secretion system.PLoS pathogens · 2011Article
- Archaeal flagellar ATPase motor shows ATP-dependent hexameric assembly and activity stimulation by specific lipid binding.The Biochemical journal · 2011Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
EpsE is an ATPase that powers transport of cholera toxin and hydrolytic enzymes through the Type II secretion (T2S) apparatus in the gram-negative bacterium, Vibrio cholerae. On the basis of structures of homologous Type II/IV secretion ATPases and our biochemical data, we believe that EpsE is active as an oligomer, likely a hexamer, and the binding, hydrolysis, and release of nucleotide cause EpsE to undergo dynamic structural changes, thus converting chemical energy to mechanical work, ultimately resulting in extracellular secretion. The conformational changes that occur as a consequence of nucleotide binding would realign conserved arginines (Arg(210), Arg(225), Arg(320), Arg(324), Arg(336), and Arg(369)) from adjoining domains and subunits to complete the active site around the bound nucleotide. Our data suggest that these arginines are essential for ATP hydrolysis, although their roles in shaping the active site of EpsE are varied. Specifically, we have shown that replacements of these arginine residues abrogate the T2S process due to a reduction of ATPase activity yet do not have any measurable effect on nucleotide binding or oligomerization of EpsE. We have further demonstrated that point mutations in the EpsE intersubunit interface also reduce ATPase activity without disrupting oligomerization, strengthening the idea that residues from multiple subunits must precisely interact in order for EpsE to be sufficiently active to support T2S. Our findings suggest that the action of EpsE is similar to that of other Type II/IV secretion ATPase family members, and thus these results may be widely applicable to the family as a whole.
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