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| | <StructureSection load='6p4x' size='340' side='right'caption='[[6p4x]], [[Resolution|resolution]] 3.59Å' scene=''> | | <StructureSection load='6p4x' size='340' side='right'caption='[[6p4x]], [[Resolution|resolution]] 3.59Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6p4x]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. 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 [http://proteopedia.org/fgij/fg.htm?mol=6P4X FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLK1, HOR3, YCL040W, YCL312, YCL40W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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='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'>[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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6p4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p4x OCA], [http://pdbe.org/6p4x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p4x RCSB], [http://www.ebi.ac.uk/pdbsum/6p4x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p4x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6p4x" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6p4x" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Hexokinase 3D structures|Hexokinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | |
| - | [[Category: Glucokinase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Garner, E C]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Murray, A W]] | + | [[Category: Garner EC]] |
| - | [[Category: Stoddard, P R]] | + | [[Category: Murray AW]] |
| - | [[Category: Actin atpase]] | + | [[Category: Stoddard PR]] |
| - | [[Category: Glycolysis]]
| + | |
| - | [[Category: Hexokinase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Albig W, Entian KD. Structure of yeast glucokinase, a strongly diverged specific aldo-hexose-phosphorylating isoenzyme. Gene. 1988 Dec 15;73(1):141-52. PMID:3072253
- ↑ Stoddard PR, Lynch EM, Farrell DP, Dosey AM, DiMaio F, Williams TA, Kollman JM, Murray AW, Garner EC. Polymerization in the actin ATPase clan regulates hexokinase activity in yeast. Science. 2020 Feb 28;367(6481):1039-1042. doi: 10.1126/science.aay5359. PMID:32108112 doi:http://dx.doi.org/10.1126/science.aay5359
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