Structure of UBE2Z Enzyme Provides Functional ...
Type de document :
Article dans une revue scientifique
DOI :
PMID :
URL permanente :
Titre :
Structure of UBE2Z Enzyme Provides Functional Insight into Specificity in the FAT10 Protein Conjugation Machinery
Auteur(s) :
Schelpe, Julien [Auteur]
Monte, Didier [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Dewitte, Frederique [Auteur]
Sixma, Titia K. [Auteur]
Rucktooa, Prakash [Auteur]
Monte, Didier [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Dewitte, Frederique [Auteur]
Sixma, Titia K. [Auteur]
Rucktooa, Prakash [Auteur]
Titre de la revue :
The Journal of biological chemistry
Nom court de la revue :
J. Biol. Chem.
Numéro :
291
Pagination :
630-639
Date de publication :
2016-01-08
ISSN :
1083-351X
Mot(s)-clé(s) en anglais :
Protein Structure, Tertiary
post-translational modification (PTM)
Ubiquitin
Amino Acid Sequence
Crystal Structure
FAT10
UBL conjugation
Protein Structure, Secondary
Peptides
X-ray Crystallography
Substrate Specificity
Molecular Sequence Data
UBE2Z
Mutant Proteins
ubiquitylation (ubiquitination)
Ubiquitin-Activating Enzymes
ubiquitin-conjugating enzyme (E2 enzyme)
Kinetics
Ubiquitin-Conjugating Enzymes
post-translational modification (PTM)
Ubiquitin
Amino Acid Sequence
Crystal Structure
FAT10
UBL conjugation
Protein Structure, Secondary
Peptides
X-ray Crystallography
Substrate Specificity
Molecular Sequence Data
UBE2Z
Mutant Proteins
ubiquitylation (ubiquitination)
Ubiquitin-Activating Enzymes
ubiquitin-conjugating enzyme (E2 enzyme)
Kinetics
Ubiquitin-Conjugating Enzymes
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
FAT10 conjugation, a post-translational modification analogous to ubiquitination, specifically requires UBA6 and UBE2Z as its activating (E1) and conjugating (E2) enzymes. Interestingly, these enzymes can also function in ...
Lire la suite >FAT10 conjugation, a post-translational modification analogous to ubiquitination, specifically requires UBA6 and UBE2Z as its activating (E1) and conjugating (E2) enzymes. Interestingly, these enzymes can also function in ubiquitination. We have determined the crystal structure of UBE2Z and report how the different domains of this E2 enzyme are organized. We further combine our structural data with mutational analyses to understand how specificity is achieved in the FAT10 conjugation pathway. We show that specificity toward UBA6 and UBE2Z lies within the C-terminal CYCI tetrapeptide in FAT10. We also demonstrate that this motif slows down transfer rates for FAT10 from UBA6 onto UBE2Z.Lire moins >
Lire la suite >FAT10 conjugation, a post-translational modification analogous to ubiquitination, specifically requires UBA6 and UBE2Z as its activating (E1) and conjugating (E2) enzymes. Interestingly, these enzymes can also function in ubiquitination. We have determined the crystal structure of UBE2Z and report how the different domains of this E2 enzyme are organized. We further combine our structural data with mutational analyses to understand how specificity is achieved in the FAT10 conjugation pathway. We show that specificity toward UBA6 and UBE2Z lies within the C-terminal CYCI tetrapeptide in FAT10. We also demonstrate that this motif slows down transfer rates for FAT10 from UBA6 onto UBE2Z.Lire moins >
Langue :
Anglais
Établissement(s) :
CNRS
Université de Lille
Université de Lille
Équipe(s) de recherche :
Biologie structurale et intégrative
Date de dépôt :
2020-02-12T15:11:31Z