3W0L

The crystal structure of Xenopus Glucokinase and Glucokinase Regulatory Protein complex

3W0L の概要

• エントリーDOI: 10.2210/pdb3w0l/pdb
• 分子名称: Glucokinase, Glucokinase regulatory protein, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: aba sandwich, typical hexokanse fold, kinase, sugar binding, transferase-transferase inhibitor complex, transferase/transferase inhibitor
• 由来する生物種: Xenopus laevis (African clawed frog); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 240865.78

構造登録者

Choi, J.M.,Seo, M.H.,Kyeong, H.H.,Kim, E.,Kim, H.S. (登録日: 2012-10-31, 公開日: 2013-07-17, 最終更新日: 2023-11-08)

主引用文献

Choi, J.M.,Seo, M.H.,Kyeong, H.H.,Kim, E.,Kim, H.S.
Molecular basis for the role of glucokinase regulatory protein as the allosteric switch for glucokinase
Proc.Natl.Acad.Sci.USA, 110:10171-10176, 2013

PubMed Abstract: Glucokinase (GK) is a monomeric allosteric enzyme and plays a pivotal role in blood glucose homeostasis. GK is regulated by GK regulatory protein (GKRP), and indirectly by allosteric effectors of GKRP. Despite the critical roles of GK and GKRP, the molecular basis for the allosteric regulation mechanism of GK by GKRP remains unclear. We determined the crystal structure of Xenopus GK and GKRP complex in the presence of fructose-6-phosphate at 2.9 Å. GKRP binds to a super-open conformation of GK mainly through hydrophobic interaction, inhibiting the GK activity by locking a small domain of GK. We demonstrate the molecular mechanism for the modulation of GK activity by allosteric effectors of GKRP. Importantly, GKRP releases GK in a sigmoidal manner in response to glucose concentration by restricting a structural rearrangement of the GK small domain via a single ion pair. We find that GKRP acts as an allosteric switch for GK in blood glucose control by the liver.

PubMed: 23733961
DOI: 10.1073/pnas.1300457110

実験手法

X-RAY DIFFRACTION (2.92 Å)