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-Structure paper
Title | Polymerization in the actin ATPase clan regulates hexokinase activity in yeast. |
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Journal, issue, pages | Science, Vol. 367, Issue 6481, Page 1039-1042, Year 2020 |
Publish date | Feb 28, 2020 |
Authors | Patrick R Stoddard / Eric M Lynch / Daniel P Farrell / Annie M Dosey / Frank DiMaio / Tom A Williams / Justin M Kollman / Andrew W Murray / Ethan C Garner / |
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 ...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. |
External links | Science / PubMed:32108112 / PubMed Central |
Methods | EM (helical sym.) / X-ray diffraction |
Resolution | 3.59 - 3.8 Å |
Structure data | EMDB-20309, PDB-6pdt: PDB-6p4x: |
Chemicals | ChemComp-PO4: ChemComp-GLC: ChemComp-MG: ChemComp-ATP: |
Source |
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Keywords | TRANSFERASE / hexokinase / actin atpase / glycolysis / filament |