5a4p

Structure of UBE2Z provides functional insight into specificity in the FAT10 conjugation machinery

spinqualitylabelsall models 5a4p, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5a4p is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: MLI, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function UBE2Z_HUMAN Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity). Specific substrate for UBA6, not charged with ubiquitin by UBE1. May be involved in apoptosis regulation.[PROSITE-ProRule:PRU00388] Publication Abstract from PubMed 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 towards UBA6 and UBE2Z lies within the C-terminal CYCI tetra-peptide in FAT10. We also demonstrate that this motif slows down transfer rates for FAT10 from UBA6 onto UBE2Z. Structure of UBE2Z provides functional insight into specificity in the FAT10 conjugation machinery.,Schelpe J, Monte D, Dewitte F, Sixma TK, Rucktooa P J Biol Chem. 2015 Nov 10. pii: jbc.M115.671545. PMID:26555268 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also 3D structures of ubiquitin conjugating enzyme

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