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Entropic pressure controls the oligomerization of the Vibrio cholerae ParD2 antitoxin
Author(s) -
Garcia-Rodriguez Gabriela,
Girardin Yana,
Volkov Alexander N.,
Singh Ranjan Kumar,
Muruganandam Gopinath,
Van Dyck Jeroen,
Sobott Frank,
Versées Wim,
Charlier Daniel,
Loris Remy
Publication year - 2021
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798321004873
Subject(s) - vibrio cholerae , antitoxin , chemistry , crystallography , cholera toxin , hydrogen bond , oligomer , biophysics , stereochemistry , biology , toxin , biochemistry , microbiology and biotechnology , polymer chemistry , genetics , molecule , bacteria , organic chemistry
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 ( Vc ParD2) 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 Vc ParD2 dimers mimics the arrangement of Streptococcus agalactiae CopG dimers on their operator and allows an extended operator to wrap around the Vc ParD2 oligomer.