6p4x
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of the S. cerevisiae glucokinase, Glk1== | |
| + | <StructureSection load='6p4x' size='340' side='right'caption='[[6p4x]], [[Resolution|resolution]] 3.59Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6p4x]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P4X FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.59Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6p4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p4x OCA], [https://pdbe.org/6p4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p4x RCSB], [https://www.ebi.ac.uk/pdbsum/6p4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p4x ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://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> |
| - | [[Category: Garner | + | <div class="pdbe-citations 6p4x" style="background-color:#fffaf0;"></div> |
| - | [[Category: Murray | + | |
| - | [[Category: Stoddard | + | ==See Also== |
| + | *[[Hexokinase 3D structures|Hexokinase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae S288C]] | ||
| + | [[Category: Garner EC]] | ||
| + | [[Category: Murray AW]] | ||
| + | [[Category: Stoddard PR]] | ||
Current revision
Crystal Structure of the S. cerevisiae glucokinase, Glk1
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