7QF7

Orthorhombic crystal structure of PTG CBM21 in complex with beta-cyclodextrin

7QF7 の概要

• エントリーDOI: 10.2210/pdb7qf7/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900012
• 分子名称: Protein phosphatase 1 regulatory subunit 3C, Cycloheptakis-(1-4)-(alpha-D-glucopyranose), SODIUM ION, ... (4 entities in total)
• 機能のキーワード: carbohydrate binding, immunoglobulin-like fold, sugar binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16823.52

構造登録者

Semrau, M.S.,Storici, P.,Lolli, G. (登録日: 2021-12-04, 公開日: 2022-11-02, 最終更新日: 2024-01-31)

主引用文献

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

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: 36261419
DOI: 10.1038/s41467-022-33693-z

実験手法

X-RAY DIFFRACTION (1.47 Å)