7QM2
Crystal structure of the PP1/PTG/beta-cyclodextrin ternary complex
Summary for 7QM2
| Entry DOI | 10.2210/pdb7qm2/pdb |
| Related | 7QF7 7QFA 7QFB |
| Related PRD ID | PRD_900012 |
| Descriptor | Serine/threonine-protein phosphatase PP1-alpha catalytic subunit, Protein phosphatase 1 regulatory subunit 3C, Cycloheptakis-(1-4)-(alpha-D-glucopyranose), ... (4 entities in total) |
| Functional Keywords | phosphatase, carbohydrate binding, hydrolase |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 116709.78 |
| Authors | Semrau, M.S.,Storici, P.,Lolli, G. (deposition date: 2021-12-20, release date: 2022-11-02, Last modification date: 2024-01-31) |
| Primary citation | Semrau, M.S.,Giachin, G.,Covaceuszach, S.,Cassetta, A.,Demitri, N.,Storici, P.,Lolli, G. Molecular architecture of the glycogen- committed PP1/PTG holoenzyme. Nat Commun, 13:6199-6199, 2022 Cited by PubMed Abstract: The delicate alternation between glycogen synthesis and degradation is governed by the interplay between key regulatory enzymes altering the activity of glycogen synthase and phosphorylase. Among these, the PP1 phosphatase promotes glycogenesis while inhibiting glycogenolysis. PP1 is, however, a master regulator of a variety of cellular processes, being conveniently directed to each of them by scaffolding subunits. PTG, Protein Targeting to Glycogen, addresses PP1 action to glycogen granules. In Lafora disease, the most aggressive pediatric epilepsy, genetic alterations leading to PTG accumulation cause the deposition of insoluble polyglucosans in neurons. Here, we report the crystallographic structure of the ternary complex PP1/PTG/carbohydrate. We further refine the mechanism of the PTG-mediated PP1 recruitment to glycogen by identifying i) an unusual combination of recruitment sites, ii) their contributions to the overall binding affinity, and iii) the conformational heterogeneity of this complex by in solution SAXS analyses. PubMed: 36261419DOI: 10.1038/s41467-022-33693-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.685 Å) |
Structure validation
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