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Entropic pressure controls olgomerization of Vibrio cholerae ParD2 antitoxin

Journal Contribution - Journal Article

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.
Journal: Acta Crystallographica. Section D, Biological Crystallography
ISSN: 0907-4449
Issue: Pt 7
Volume: 77
Pages: 904-920
Number of pages: 17
Publication year:2021
Keywords:Toxin-Antitoxin module, DNA binding, Transcription regulation, Intrinsicallydisordered protein, Protein oligomerization, X-ray crystallography, SAXS, Oligomer interface, Protein-DNA interaction, Quaternary structure, Biochemistry/biophysics/molecular biology, Physics of solids, fluids and plasmas, Biochemistry/biophysics/molecular biology, Physics of solids, fluids and plasmas