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Open data
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Basic information
Entry | Database: PDB / ID: 6p4x | |||||||||
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Title | Crystal Structure of the S. cerevisiae glucokinase, Glk1 | |||||||||
![]() | Glucokinase-1 | |||||||||
![]() | TRANSFERASE / hexokinase / actin atpase / glycolysis | |||||||||
Function / homology | ![]() Regulation of Glucokinase by Glucokinase Regulatory Protein / glucokinase / Glycolysis / fructokinase activity / carbohydrate phosphorylation / glucokinase activity / mannose metabolic process / glucose 6-phosphate metabolic process / D-glucose binding / glucose import ...Regulation of Glucokinase by Glucokinase Regulatory Protein / glucokinase / Glycolysis / fructokinase activity / carbohydrate phosphorylation / glucokinase activity / mannose metabolic process / glucose 6-phosphate metabolic process / D-glucose binding / glucose import / intracellular glucose homeostasis / Neutrophil degranulation / glycolytic process / glucose metabolic process / mitochondrion / ATP binding / plasma membrane / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Stoddard, P.R. / Garner, E.C. / Murray, A.W. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Polymerization in the actin ATPase clan regulates hexokinase activity in yeast. 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 / ![]() ![]() 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. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.2 MB | Display | ![]() |
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PDB format | ![]() | 961.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 502.8 KB | Display | ![]() |
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Full document | ![]() | 591.5 KB | Display | |
Data in XML | ![]() | 109 KB | Display | |
Data in CIF | ![]() | 143.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6pdtC ![]() 1ig8S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Assembly
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Ens-ID: 1
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