6pdt
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==cryoEM structure of yeast glucokinase filament== | |
+ | <StructureSection load='6pdt' size='340' side='right'caption='[[6pdt]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6pdt]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PDT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PDT FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6pdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pdt OCA], [http://pdbe.org/6pdt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pdt RCSB], [http://www.ebi.ac.uk/pdbsum/6pdt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pdt ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/HXKG_YEAST HXKG_YEAST]] Two isoenzymes, hexokinase-1 and hexokinase-2, can phosphorylate keto- and aldohexoses in yeast, whereas a third isoenzyme, GLK, is specific for aldohexoses. All glucose phosphorylating enzymes are involved in glucose uptake.<ref>PMID:3072253</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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 Saccharomyces cerevisiae 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. | ||
- | + | Polymerization in the actin ATPase clan regulates hexokinase activity in yeast.,Stoddard PR, Lynch EM, Farrell DP, Dosey AM, DiMaio F, Williams TA, Kollman JM, Murray AW, Garner EC Science. 2020 Feb 28;367(6481):1039-1042. doi: 10.1126/science.aay5359. PMID:32108112<ref>PMID:32108112</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 6pdt" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Glucokinase]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Dosey, A M]] | ||
+ | [[Category: Farrell, D P]] | ||
+ | [[Category: Kollman, J M]] | ||
+ | [[Category: Lynch, E M]] | ||
+ | [[Category: Stoddard, P R]] | ||
+ | [[Category: Filament]] | ||
+ | [[Category: Transferase]] |
Revision as of 07:23, 11 March 2020
cryoEM structure of yeast glucokinase filament
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