2YB6
Native human Rad6
Summary for 2YB6
| Entry DOI | 10.2210/pdb2yb6/pdb |
| Related | 1JAS 1NXA 2Y4W 2YBF |
| Descriptor | UBIQUITIN-CONJUGATING ENZYME E2 B, BETA-MERCAPTOETHANOL, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | ligase, translesion synthesis, ubiquitin chain synthesis |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Cell membrane (By similarity): P63146 |
| Total number of polymer chains | 1 |
| Total formula weight | 17441.87 |
| Authors | Hibbert, R.G.,Sixma, T.K. (deposition date: 2011-03-02, release date: 2011-04-20, Last modification date: 2023-12-20) |
| Primary citation | Hibbert, R.G.,Huang, A.,Boelens, R.,Sixma, T.K. E3 Ligase Rad18 Promotes Monoubiquitination Rather Than Ubiquitin Chain Formation by E2 Enzyme Rad6. Proc.Natl.Acad.Sci.USA, 108:5590-, 2011 Cited by PubMed Abstract: In ubiquitin conjugation, different combinations of E2 and E3 enzymes catalyse either monoubiquitination or ubiquitin chain formation. The E2/E3 complex Rad6/Rad18 exclusively monoubiquitinates the proliferating cell nuclear antigen (PCNA) to signal for "error prone" DNA damage tolerance, whereas a different set of conjugation enzymes is required for ubiquitin chain formation on PCNA. Here we show that human E2 enzyme Rad6b is intrinsically capable of catalyzing ubiquitin chain formation. This activity is prevented during PCNA ubiquitination by the interaction of Rad6 with E3 enzyme Rad18. Using NMR and X-ray crystallography we show that the R6BD of Rad18 inhibits this activity by competing with ubiquitin for a noncovalent "backside" binding site on Rad6. Our findings provide mechanistic insights into how E3 enzymes can regulate the ubiquitin conjugation process. PubMed: 21422291DOI: 10.1073/PNAS.1017516108 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
Download full validation report
