Projects per year
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 language | English |
---|---|
Pages (from-to) | 904-920 |
Number of pages | 17 |
Journal | Acta Crystallographica Section D: Structural Biology (2016- ) |
Volume | 77 |
Issue number | Pt 7 |
DOIs | |
Publication status | Published - 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
Fingerprint
Dive into the research topics of 'Entropic pressure controls olgomerization of Vibrio cholerae ParD2 antitoxin'. Together they form a unique fingerprint.-
FWOAL967: Structural and thermodynamic dissection of fuzzy protein-DNA interactions in a prokaryotic transcription factor
1/01/20 → 31/12/23
Project: Fundamental
-
FWOTM961: Mechanism of Gyrase-poisoning by ParE and its rejuvenation by ParD
1/11/19 → 31/10/21
Project: Fundamental
-
FWOAL831: Regulation of persistence by the paaAR-paaA2-parE2 and cog4197-duf1019 operons from E. coli O157
1/01/17 → 31/12/20
Project: Fundamental
-
Prokaryote toxin-antitoxin modules: complex regulation of an unclear function
De Bruyn, P., Girardin, Y. & Loris, R., Jun 2021, In: Protein Sci. 30, 6, p. 1103-1113 11 p.Research output: Contribution to journal › Article › peer-review
Open AccessFile10 Citations (Scopus)115 Downloads (Pure) -
Regulatory mechanisms behind the activities of bacterial HEPN ribonuclease RnlA and ParE2 gyrase poison
Garcia Rodriguez, G., 2020Research output: Thesis › PhD Thesis
Equipment
-
X-Ray Generator
Facility/equipment: Equipment