1Z0M

the glycogen-binding domain of the AMP-activated protein kinase beta1 subunit

1Z0M の概要

• エントリーDOI: 10.2210/pdb1z0m/pdb
• 関連するPDBエントリー: 1Z0N
• 関連するBIRD辞書のPRD_ID: PRD_900012
• 分子名称: 5'-AMP-activated protein kinase, beta-1 subunit, Cycloheptakis-(1-4)-(alpha-D-glucopyranose) (3 entities in total)
• 機能のキーワード: beta sandwich, sugar binding protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 36183.34

構造登録者

Polekhina, G.,Gupta, A.,van Denderen, B.J.,Feil, S.C.,Kemp, B.E.,Stapleton, D.,Parker, M.W. (登録日: 2005-03-02, 公開日: 2005-10-25, 最終更新日: 2024-03-13)

主引用文献

Polekhina, G.,Gupta, A.,van Denderen, B.J.,Feil, S.C.,Kemp, B.E.,Stapleton, D.,Parker, M.W.
Structural Basis for Glycogen Recognition by AMP-Activated Protein Kinase.
Structure, 13:1453-1462, 2005

PubMed Abstract: AMP-activated protein kinase (AMPK) coordinates cellular metabolism in response to energy demand as well as to a variety of stimuli. The AMPK beta subunit acts as a scaffold for the alpha catalytic and gamma regulatory subunits and targets the AMPK heterotrimer to glycogen. We have determined the structure of the AMPK beta glycogen binding domain in complex with beta-cyclodextrin. The structure reveals a carbohydrate binding pocket that consolidates all known aspects of carbohydrate binding observed in starch binding domains into one site, with extensive contact between several residues and five glucose units. beta-cyclodextrin is held in a pincer-like grasp with two tryptophan residues cradling two beta-cyclodextrin glucose units and a leucine residue piercing the beta-cyclodextrin ring. Mutation of key beta-cyclodextrin binding residues either partially or completely prevents the glycogen binding domain from binding glycogen. Modeling suggests that this binding pocket enables AMPK to interact with glycogen anywhere across the carbohydrate's helical surface.

PubMed: 16216577
DOI: 10.1016/j.str.2005.07.008

実験手法

X-RAY DIFFRACTION (1.91 Å)