ArticleActa crystallographica. Section D, Structural biology2021
Entropic pressure controls the oligomerization of the Vibrio cholerae ParD2 antitoxin.
Article in Acta crystallographica. Section D, Structural biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 6 citations in OpenAlex.
- Toxin:antitoxin ratio sensing autoregulation of theScience advances · 2024Article
- Toxin-antitoxin systems in pathogenic3 Biotech · 2022Review
- Structural insights into the PrpTA toxin-antitoxin system inFrontiers in microbiology · 2022Article
- Insights into the Neutralization and DNA Binding of Toxin-Antitoxin System ParEMicroorganisms · 2021Article
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
ParD2 is the antitoxin component of the parDE2 toxin-antitoxin module from Vibrio cholerae and consists of an ordered DNA-binding domain followed by an intrinsically disordered ParE-neutralizing domain. In the absence of the C-terminal intrinsically disordered protein (IDP) domain, V. cholerae ParD2 (VcParD2) crystallizes as a doughnut-shaped hexadecamer formed by the association of eight dimers. This assembly is stabilized via hydrogen bonds and salt bridges rather than by hydrophobic contacts. In solution, oligomerization of the full-length protein is restricted to a stable, open decamer or dodecamer, which is likely to be a consequence of entropic pressure from the IDP tails. The relative positioning of successive VcParD2 dimers mimics the arrangement of Streptococcus agalactiae CopG dimers on their operator and allows an extended operator to wrap around the VcParD2 oligomer.
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