Structure of UBE2Z Enzyme Provides Functional Insight into Specificity in the FAT10 Protein Conjugation Machinery
Résumé
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.
Mots clés
Protein Structure
Tertiary
post-translational modification (PTM)
Ubiquitin
Amino Acid Sequence
Crystal Structure
FAT10
UBL conjugation
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
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