Entropic pressure controls the oligomerization of the Vibrio cholerae ParD2 antitoxin
| Autor: | Yana Girardin, Wim Versées, Frank Sobott, Alexander N. Volkov, Jeroen Van Dyck, Remy Loris, Ranjan Kumar Singh, Gabriela Garcia-Rodriguez, Gopinath Muruganandam, Daniel Charlier |
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| Rok vydání: | 2021 |
| Předmět: |
ParD2
quaternary structure toxin–antitoxin module medicine.disease_cause Intrinsically disordered proteins Oligomer 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Structural Biology medicine Biology Vibrio cholerae 030304 developmental biology 0303 health sciences protein oligomers 030306 microbiology COPG Hydrogen bond Chemistry Physics Research Papers oligomer interface DNA-Binding Proteins protein–DNA interactions Crystallography Dodecameric protein Protein quaternary structure Antitoxins intrinsically disordered proteins Antitoxin Protein Multimerization transcription regulation |
| Zdroj: | Acta Crystallographica. Section D, Structural Biology Acta crystallographica. Section D, Structural biology |
| ISSN: | 2059-7983 |
| Popis: | ParD2 forms an open oligomer in solution, the size of which is limited by the presence of an intrinsically disordered tail. In the absence of this tail, ParD2 forms a circular hexadecamer. 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. |
| Databáze: | OpenAIRE |
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