5A4P
Structure of UBE2Z provides functional insight into specificity in the FAT10 conjugation machinery
Summary for 5A4P
| Entry DOI | 10.2210/pdb5a4p/pdb |
| Descriptor | UBIQUITIN-CONJUGATING ENZYME E2 Z, MALONATE ION, DI(HYDROXYETHYL)ETHER, ... (4 entities in total) |
| Functional Keywords | ligase, e2 enzyme, fat10 conjugation, ubiquitin conjugation |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Cytoplasm : Q9H832 |
| Total number of polymer chains | 1 |
| Total formula weight | 38971.55 |
| Authors | Schelpe, J.,Monte, D.,Dewitte, F.,Sixma, T.K.,Rucktooa, P. (deposition date: 2015-06-11, release date: 2015-11-18, Last modification date: 2024-01-10) |
| Primary citation | Schelpe, J.,Monte, D.,Dewitte, F.,Sixma, T.K.,Rucktooa, P. Structure of Ube2Z Provides Functional Insight Into Specificity in the Fat10 Conjugation Machinery J.Biol.Chem., 291:630-, 2016 Cited by PubMed Abstract: 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. PubMed: 26555268DOI: 10.1074/JBC.M115.671545 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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