Entropic pressure controls olgomerization of Vibrio cholerae ParD2 antitoxin

Gabriela Garcia Rodriguez, Yana Girardin, Oleksandr Volkov, Ranjan Kumar Singh, Gopinath Muruganandam, Jeroen Van Dyck, Frank Sobott, Wim Versées, Daniel Charlier, Remy Loris

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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 absence of the C-terminal IDP domain, 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 hydrophobic contacts. In solution, oligomerization of the full-length protein is restricted to a stable, open 10-mer or 12-mer, likely as 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 for an extended operator to wrap around the VcParD2 oligomer.
Original languageEnglish
Pages (from-to)904-920
Number of pages17
JournalActa Crystallographica Section D: Structural Biology (2016- )
Volume77
Issue numberPt 7
DOIs
Publication statusPublished - 18 Jun 2021

Keywords

  • Toxin-Antitoxin module
  • DNA binding
  • Transcription regulation
  • Intrinsicallydisordered protein
  • Protein oligomerization
  • X-ray crystallography
  • SAXS
  • Oligomer interface
  • Protein-DNA interaction
  • Quaternary structure

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