6U75
Crystal Structure of S. Cerevisiae SUMO E3 Ligase SIZ2
Summary for 6U75
| Entry DOI | 10.2210/pdb6u75/pdb |
| Descriptor | E3 SUMO-protein ligase SIZ2, ZINC ION (3 entities in total) |
| Functional Keywords | sumo, signal transduction, replication, ring e3, pias, siz, ubiquitin, ubc9, ligase, metal-binding, nucleus, phosphoprotein, ubl conjugation pathway, zinc-finger |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 61649.71 |
| Authors | Lima, C.D.,Cappadocia, L. (deposition date: 2019-08-31, release date: 2020-10-28, Last modification date: 2023-10-11) |
| Primary citation | Cappadocia, L.,Kochanczyk, T.,Lima, C.D. DNA asymmetry promotes SUMO modification of the single-stranded DNA-binding protein RPA. Embo J., 40:e103787-e103787, 2021 Cited by PubMed Abstract: Repair of DNA double-stranded breaks by homologous recombination (HR) is dependent on DNA end resection and on post-translational modification of repair factors. In budding yeast, single-stranded DNA is coated by replication protein A (RPA) following DNA end resection, and DNA-RPA complexes are then SUMO-modified by the E3 ligase Siz2 to promote repair. Here, we show using enzymatic assays that DNA duplexes containing 3' single-stranded DNA overhangs increase the rate of RPA SUMO modification by Siz2. The SAP domain of Siz2 binds DNA duplexes and makes a key contribution to this process as highlighted by models and a crystal structure of Siz2 and by assays performed using protein mutants. Enzymatic assays performed using DNA that can accommodate multiple RPA proteins suggest a model in which the SUMO-RPA signal is amplified by successive rounds of Siz2-dependent SUMO modification of RPA and dissociation of SUMO-RPA at the junction between single- and double-stranded DNA. Our results provide insights on how DNA architecture scaffolds a substrate and E3 ligase to promote SUMO modification in the context of DNA repair. PubMed: 34585421DOI: 10.15252/embj.2019103787 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.63 Å) |
Structure validation
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