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| <StructureSection load='1s4e' size='340' side='right'caption='[[1s4e]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='1s4e' size='340' side='right'caption='[[1s4e]], [[Resolution|resolution]] 2.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1s4e]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S4E OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1S4E FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1s4e]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S4E FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.9Å</td></tr> |
| <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GALK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 ATCC 43587])</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=1s4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s4e OCA], [https://pdbe.org/1s4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s4e RCSB], [https://www.ebi.ac.uk/pdbsum/1s4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s4e ProSAT]</span></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Galactokinase Galactokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.6 2.7.1.6] </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=1s4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s4e OCA], [http://pdbe.org/1s4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s4e RCSB], [http://www.ebi.ac.uk/pdbsum/1s4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s4e ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/GAL1_PYRFU GAL1_PYRFU]] Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). Is very specific for its substrate, since it is not able to use D-glucose, D-fructose, D-mannose, 2-deoxy-D-glucose, and D-glucosamine as substrates.<ref>PMID:11978175</ref> | | [https://www.uniprot.org/uniprot/GAL1_PYRFU GAL1_PYRFU] Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). Is very specific for its substrate, since it is not able to use D-glucose, D-fructose, D-mannose, 2-deoxy-D-glucose, and D-glucosamine as substrates.<ref>PMID:11978175</ref> |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1s4e ConSurf]. | | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1s4e ConSurf]. |
| <div style="clear:both"></div> | | <div style="clear:both"></div> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Galactokinase (GalK) catalyses the first step of the Leloir pathway of galactose metabolism, the ATP-dependent phosphorylation of galactose to galactose-1-phosphate. In man, defects in galactose metabolism can result in disorders with severe clinical consequences, and deficiencies in galactokinase have been linked with the development of cataracts within the first few months of life. The crystal structure of GalK from Pyrococcus furiosus in complex with MgADP and galactose has been determined to 2.9 A resolution to provide insights into the substrate specificity and catalytic mechanism of the enzyme. The structure consists of two domains with the active site in a cleft at the domain interface. Inspection of the substrate binding pocket identifies the amino acid residues involved in galactose and nucleotide binding and points to both structural and mechanistic similarities with other enzymes of the GHMP kinase superfamily to which GalK belongs. Comparison of the sequence of the Gal3p inducer protein, which is related to GalK and which forms part of the transcriptional activation of the GAL gene cluster in the yeast Saccharomyces cerevisiae, has led to an understanding of the molecular basis of galactose and nucleotide recognition. Finally, the structure has enabled us to further our understanding on the functional consequences of mutations in human GalK which cause galactosemia.
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| Substrate specificity and mechanism from the structure of Pyrococcus furiosus galactokinase.,Hartley A, Glynn SE, Barynin V, Baker PJ, Sedelnikova SE, Verhees C, de Geus D, van der Oost J, Timson DJ, Reece RJ, Rice DW J Mol Biol. 2004 Mar 19;337(2):387-98. PMID:15003454<ref>PMID:15003454</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 1s4e" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Atcc 43587]]
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| [[Category: Galactokinase]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Baker, P J]] | | [[Category: Pyrococcus furiosus]] |
| [[Category: Barynin, V]] | | [[Category: Baker PJ]] |
| [[Category: Geus, D de]] | | [[Category: Barynin V]] |
| [[Category: Glynn, S E]] | | [[Category: Glynn SE]] |
| [[Category: Hartley, A]] | | [[Category: Hartley A]] |
| [[Category: Oost, J van der]]
| | [[Category: Reece RJ]] |
| [[Category: Reece, R J]] | | [[Category: Rice DW]] |
| [[Category: Rice, D W]] | | [[Category: Sedelnikova SE]] |
| [[Category: Sedelnikova, S E]] | | [[Category: Timson DJ]] |
| [[Category: Timson, D J]] | | [[Category: Verhees C]] |
| [[Category: Verhees, C]] | | [[Category: De Geus D]] |
| [[Category: Ghmp kinase superfamily]] | | [[Category: Van der Oost J]] |
| [[Category: P-loop]] | |
| [[Category: Transferase]]
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