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| | <StructureSection load='3b8a' size='340' side='right'caption='[[3b8a]], [[Resolution|resolution]] 2.95Å' scene=''> | | <StructureSection load='3b8a' size='340' side='right'caption='[[3b8a]], [[Resolution|resolution]] 2.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3b8a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B8A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3B8A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3b8a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B8A FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.95Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hexokinase Hexokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.1 2.7.1.1] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3b8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b8a OCA], [http://pdbe.org/3b8a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3b8a RCSB], [http://www.ebi.ac.uk/pdbsum/3b8a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3b8a ProSAT]</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=3b8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b8a OCA], [https://pdbe.org/3b8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b8a RCSB], [https://www.ebi.ac.uk/pdbsum/3b8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b8a ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HXKA_YEAST HXKA_YEAST] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hexokinase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Saccharomyces cerevisiae]] | | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Bleicher, L]] | + | [[Category: Bleicher L]] |
| - | [[Category: Cupri, F]] | + | [[Category: Cupri F]] |
| - | [[Category: Kuser, P]] | + | [[Category: Kuser P]] |
| - | [[Category: Polikarpov, I]] | + | [[Category: Polikarpov I]] |
| - | [[Category: Allosteric enzyme]]
| + | |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Glycolysis]]
| + | |
| - | [[Category: Induced fit]]
| + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
HXKA_YEAST
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Hexokinase is the first enzyme in the glycolytic pathway that catalyzes the transfer of a phosphoryl group from ATP to glucose to form glucose-6-phosphate and ADP. Two yeast hexokinase isozymes are known, namely PI and PII. Here we redetermined the crystal structure of yeast hexokinase PI from Saccharomyces cerevisiae as a complex with its substrate, glucose, and refined it at 2.95 A resolution. Comparison of the holo-PI yeast hexokinase and apo-hexokinase structures shows in detail the rigid body domain closure and specific loop movements as glucose binds and sheds more light on structural basis of the "induced fit" mechanism of reaction in the HK enzymatic action. We also performed statistical coupling analysis of the hexokinase family, which reveals two co-evolved continuous clusters of amino acid residues and shows that the evolutionary coupled amino acid residues are mostly confined to the active site and the hinge region, further supporting the importance of these parts of the protein for the enzymatic catalysis. Proteins 2008. (c) 2008 Wiley-Liss, Inc.
Crystal structure of yeast hexokinase PI in complex with glucose: A classical "induced fit" example revised.,Kuser P, Cupri F, Bleicher L, Polikarpov I Proteins. 2008 Feb 7;. PMID:18260108[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kuser P, Cupri F, Bleicher L, Polikarpov I. Crystal structure of yeast hexokinase PI in complex with glucose: A classical "induced fit" example revised. Proteins. 2008 Feb 7;. PMID:18260108 doi:10.1002/prot.21956
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