6PDT
cryoEM structure of yeast glucokinase filament
Summary for 6PDT
| Entry DOI | 10.2210/pdb6pdt/pdb |
| EMDB information | 20309 |
| Descriptor | Glucokinase-1, alpha-D-glucopyranose, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | filament, transferase |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Total number of polymer chains | 4 |
| Total formula weight | 224631.60 |
| Authors | Lynch, E.M.,Dosey, A.M.,Farrell, D.P.,Stoddard, P.R.,Kollman, J.M. (deposition date: 2019-06-19, release date: 2020-03-11, Last modification date: 2024-10-16) |
| Primary citation | 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 Cited by 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: 32108112DOI: 10.1126/science.aay5359 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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