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

Onderzoeksoutput: Articlepeer review

3 Citaten (Scopus)
124 Downloads (Pure)


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.
Originele taal-2English
Pagina's (van-tot)904-920
Aantal pagina's17
TijdschriftActa Crystallographica Section D: Structural Biology (2016- )
Nummer van het tijdschriftPt 7
StatusPublished - 18 jun 2021


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