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| | <StructureSection load='4b8s' size='340' side='right'caption='[[4b8s]], [[Resolution|resolution]] 2.58Å' scene=''> | | <StructureSection load='4b8s' size='340' side='right'caption='[[4b8s]], [[Resolution|resolution]] 2.58Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4b8s]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B8S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4b8s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_litoralis Thermococcus litoralis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B8S FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.58Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4b8r|4b8r]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/ADP-specific_glucokinase ADP-specific glucokinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.147 2.7.1.147] </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=4b8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b8s OCA], [https://pdbe.org/4b8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b8s RCSB], [https://www.ebi.ac.uk/pdbsum/4b8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b8s 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=4b8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b8s OCA], [https://pdbe.org/4b8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b8s RCSB], [https://www.ebi.ac.uk/pdbsum/4b8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b8s ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GLKA_THELI GLKA_THELI]] Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ADP as the phosphate donor. Can also use CDP as the phosphoryl group donor and D-glucosamine and D-1,5-anhydroglucitol as the phosphoryl group acceptor.<ref>PMID:11098152</ref>
| + | [https://www.uniprot.org/uniprot/GLKA_THELN GLKA_THELN] Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ADP as the phosphate donor. Can also use CDP as the phosphoryl group donor and D-glucosamine and D-1,5-anhydroglucitol as the phosphoryl group acceptor.<ref>PMID:11098152</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: ADP-specific glucokinase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fernandez, F J]] | + | [[Category: Thermococcus litoralis]] |
| - | [[Category: Guixe, V]] | + | [[Category: Fernandez FJ]] |
| - | [[Category: Herrera-Morande, A]] | + | [[Category: Guixe V]] |
| - | [[Category: Rivas-Pardo, J A]] | + | [[Category: Herrera-Morande A]] |
| - | [[Category: Vega, M C]] | + | [[Category: Rivas-Pardo JA]] |
| - | [[Category: Ribokinase superfamily]]
| + | [[Category: Vega MC]] |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
GLKA_THELN Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ADP as the phosphate donor. Can also use CDP as the phosphoryl group donor and D-glucosamine and D-1,5-anhydroglucitol as the phosphoryl group acceptor.[1]
Publication Abstract from PubMed
ADP-dependent glucokinases represent a unique family of kinases that belong to the ribokinase superfamily, being present mainly in hyperthermophilic archaea. For these enzymes there is no agreement about the magnitude of the structural transitions associated with ligand binding and whether they are meaningful to the function of the enzyme. We used the ADP-dependent glucokinase from Termococcus litoralis as a model to investigate the conformational changes observed in X-ray crystallographic structures upon substrate binding and to compare them with those determined in solution in order to understand their interplay with the glucokinase function. Initial velocity studies indicate that catalysis follows a sequential ordered mechanism that correlates with the structural transitions experienced by the enzyme in solution and in the crystal state. The combined data allowed us to resolve the open-closed conformational transition that accounts for the complete reaction cycle and to identify the corresponding clusters of aminoacids residues responsible for it. These results provide molecular bases for a general mechanism conserved across the ADP-dependent kinase family.
Crystal Structure, SAXS and Kinetic Mechanism of Hyperthermophilic ADP-Dependent Glucokinase from Thermococcus litoralis Reveal a Conserved Mechanism for Catalysis.,Rivas-Pardo JA, Herrera-Morande A, Castro-Fernandez V, Fernandez FJ, Vega MC, Guixe V PLoS One. 2013 Jun 20;8(6):e66687. doi: 10.1371/journal.pone.0066687. Print 2013. PMID:23818958[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Koga S, Yoshioka I, Sakuraba H, Takahashi M, Sakasegawa S, Shimizu S, Ohshima T. Biochemical characterization, cloning, and sequencing of ADP-dependent (AMP-forming) glucokinase from two hyperthermophilic archaea, Pyrococcus furiosus and Thermococcus litoralis. J Biochem. 2000 Dec;128(6):1079-85. PMID:11098152
- ↑ Rivas-Pardo JA, Herrera-Morande A, Castro-Fernandez V, Fernandez FJ, Vega MC, Guixe V. Crystal Structure, SAXS and Kinetic Mechanism of Hyperthermophilic ADP-Dependent Glucokinase from Thermococcus litoralis Reveal a Conserved Mechanism for Catalysis. PLoS One. 2013 Jun 20;8(6):e66687. doi: 10.1371/journal.pone.0066687. Print 2013. PMID:23818958 doi:10.1371/journal.pone.0066687
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