3ZGO
Re-refined structure of the human Sirt2 apoform
Summary for 3ZGO
| Entry DOI | 10.2210/pdb3zgo/pdb |
| Related | 3ZGV |
| Descriptor | NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-2, ZINC ION, HEXAETHYLENE GLYCOL, ... (7 entities in total) |
| Functional Keywords | hydrolase, nad+-dependent deacetylase, sirtuin |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 3 |
| Total formula weight | 111618.28 |
| Authors | Moniot, S.,Steegborn, C. (deposition date: 2012-12-18, release date: 2013-03-20, Last modification date: 2024-11-06) |
| Primary citation | Moniot, S.,Schutkowski, M.,Steegborn, C. Crystal Structure Analysis of Human Sirt2 and its Adp-Ribose Complex J.Struct.Biol., 182:136-, 2013 Cited by PubMed Abstract: Sirtuins are NAD(+)-dependent protein deacetylases that regulate metabolism and aging-related processes. Sirt2 is the only cytoplasmic isoform among the seven mamalian Sirtuins (Sirt1-7) and structural information concerning this isoform is limited. We crystallized Sirt2 in complex with a product analog, ADP-ribose, and solved this first crystal structure of a Sirt2 ligand complex at 2.3Å resolution. Additionally, we re-refined the structure of the Sirt2 apoform and analyzed the conformational changes associated with ligand binding to derive insights into the dynamics of the enzyme. Our analyses also provide information on Sirt2 peptide substrate binding and structural states of a Sirt2-specific protein region, and our insights and the novel Sirt2 crystal form provide helpful tools for the development of Sirt2 specific inhibitors. PubMed: 23454361DOI: 10.1016/J.JSB.2013.02.012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.63 Å) |
Structure validation
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