6ZQH
Yeast Uba1 in complex with ubiquitin
Summary for 6ZQH
| Entry DOI | 10.2210/pdb6zqh/pdb |
| Related | 3CMM |
| Descriptor | Ubiquitin-activating enzyme E1 1, Ubiquitin-40S ribosomal protein S31, BETA-MERCAPTOETHANOL, ... (6 entities in total) |
| Functional Keywords | ubiquitin, e1, ligase |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Total number of polymer chains | 4 |
| Total formula weight | 246800.36 |
| Authors | Misra, M.,Schindelin, H. (deposition date: 2020-07-09, release date: 2020-11-04, Last modification date: 2024-01-31) |
| Primary citation | Kim, R.Q.,Misra, M.,Gonzalez, A.,Tomaskovic, I.,Shin, D.,Schindelin, H.,Filippov, D.V.,Ovaa, H.,Dikic, I.,van der Heden van Noort, G.J. Development of ADPribosyl Ubiquitin Analogues to Study Enzymes Involved in Legionella Infection. Chemistry, 27:2506-2512, 2021 Cited by PubMed Abstract: Legionnaires' disease is caused by infection with the intracellularly replicating Gram-negative bacterium Legionella pneumophila. This pathogen uses an unconventional way of ubiquitinating host proteins by generating a phosphoribosyl linkage between substrate proteins and ubiquitin by making use of an ADPribosylated ubiquitin (Ub ) intermediate. The family of SidE effector enzymes that catalyze this reaction is counteracted by Legionella hydrolases, which are called Dups. This unusual ubiquitination process is important for Legionella proliferation and understanding these processes on a molecular level might prove invaluable in finding new treatments. Herein, a modular approach is used for the synthesis of triazole-linked Ub , and analogues thereof, and their affinity towards the hydrolase DupA is determined and hydrolysis rates are compared to natively linked Ub . The inhibitory effects of modified Ub on the canonical eukaryotic E1-enzyme Uba1 are investigated and rationalized in the context of a high-resolution crystal structure reported herein. Finally, it is shown that synthetic Ub analogues can be used to effectively pull-down overexpressed DupA from cell lysate. PubMed: 33075184DOI: 10.1002/chem.202004590 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.032 Å) |
Structure validation
Download full validation report
