6P4X

Crystal Structure of the S. cerevisiae glucokinase, Glk1

6P4X の概要

• エントリーDOI: 10.2210/pdb6p4x/pdb
• 分子名称: Glucokinase-1, PHOSPHATE ION (2 entities in total)
• 機能のキーワード: hexokinase, transferase, actin atpase, glycolysis
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 333912.17

構造登録者

Stoddard, P.R.,Garner, E.C.,Murray, A.W. (登録日: 2019-05-28, 公開日: 2020-03-11, 最終更新日: 2023-10-11)

主引用文献

Stoddard, P.R.,Lynch, E.M.,Farrell, D.P.,Dosey, A.M.,DiMaio, F.,Williams, T.A.,Kollman, J.M.,Murray, A.W.,Garner, E.C.
Polymerization in the actin ATPase clan regulates hexokinase activity in yeast.
Science, 367:1039-1042, 2020

PubMed Abstract: The actin fold is found in cytoskeletal polymers, chaperones, and various metabolic enzymes. Many actin-fold proteins, such as the carbohydrate kinases, do not polymerize. We found that Glk1, a glucokinase, forms two-stranded filaments with ultrastructure that is distinct from that of cytoskeletal polymers. In cells, Glk1 polymerized upon sugar addition and depolymerized upon sugar withdrawal. Polymerization inhibits enzymatic activity; the Glk1 monomer-polymer equilibrium sets a maximum rate of glucose phosphorylation regardless of Glk1 concentration. A mutation that eliminated Glk1 polymerization alleviated concentration-dependent enzyme inhibition. Yeast containing nonpolymerizing Glk1 were less fit when growing on sugars and more likely to die when refed glucose. Glk1 polymerization arose independently from other actin-related filaments and may allow yeast to rapidly modulate glucokinase activity as nutrient availability changes.

PubMed: 32108112
DOI: 10.1126/science.aay5359

実験手法

X-RAY DIFFRACTION (3.59 Å)