6DNO

Crystal structure of Protein Phosphatase 1 (PP1) bound to the muscle glycogen-targeting subunit (Gm)

6DNO の概要

• エントリーDOI: 10.2210/pdb6dno/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000212
• 分子名称: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit, Protein phosphatase 1 regulatory subunit 3A, Microcystin-LR, ... (4 entities in total)
• 機能のキーワード: inhibitor, complex, hydrolase, hydrolase-hydrolase inhibitor complex, signaling protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 38629.15

構造登録者

Choy, M.S.,Kumar, G.S.,Peti, W.,Page, R. (登録日: 2018-06-07, 公開日: 2019-01-23, 最終更新日: 2023-11-15)

主引用文献

Kumar, G.S.,Choy, M.S.,Koveal, D.M.,Lorinsky, M.K.,Lyons, S.P.,Kettenbach, A.N.,Page, R.,Peti, W.
Identification of the substrate recruitment mechanism of the muscle glycogen protein phosphatase 1 holoenzyme.
Sci Adv, 4:eaau6044-eaau6044, 2018

PubMed Abstract: Glycogen is the primary storage form of glucose. Glycogen synthesis and breakdown are tightly controlled by glycogen synthase (GYS) and phosphorylase, respectively. The enzyme responsible for dephosphorylating GYS and phosphorylase, which results in their activation (GYS) or inactivation (phosphorylase) to robustly stimulate glycogen synthesis, is protein phosphatase 1 (PP1). However, our understanding of how PP1 recruits these substrates is limited. Here, we show how PP1, together with its muscle glycogen-targeting (G) regulatory subunit, recruits and selectively dephosphorylates its substrates. Our molecular data reveal that the G carbohydrate binding module (G ), which is amino-terminal to the G PP1 binding domain, has a dual function in directing PP1 substrate specificity: It either directly recruits substrates (i.e., GYS) or recruits them indirectly by localization (via glycogen for phosphorylase). Our data provide the molecular basis for PP1 regulation by G and reveal how PP1-mediated dephosphorylation is driven by scaffolding-based substrate recruitment.

PubMed: 30443599
DOI: 10.1126/sciadv.aau6044

実験手法

X-RAY DIFFRACTION (1.45 Å)