7B22

Vibrio cholerae ParD2 Antitoxin

Summary for 7B22

• Entry DOI: 10.2210/pdb7b22/pdb
• Descriptor: Antitoxin ParD (1 entity in total)
• Functional Keywords: prokaryotic toxin-antitoxin system, intrinsically disordered proteins, rhh protein, dna binding protein, transcriptional repressor, antitoxin
• Biological source: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
• Total number of polymer chains: 8
• Total formula weight: 71782.41

Authors

Garcia-Rodriguez, G.,Loris, R. (deposition date: 2020-11-25, release date: 2021-10-06, Last modification date: 2024-01-31)

Primary citation

Garcia-Rodriguez, G.,Girardin, Y.,Volkov, A.N.,Singh, R.K.,Muruganandam, G.,Van Dyck, J.,Sobott, F.,Versees, W.,Charlier, D.,Loris, R.
Entropic pressure controls the oligomerization of the Vibrio cholerae ParD2 antitoxin.
Acta Crystallogr D Struct Biol, 77:904-920, 2021

PubMed 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.

PubMed: 34196617
DOI: 10.1107/S2059798321004873

Experimental method

X-RAY DIFFRACTION (3.08 Å)