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| | <StructureSection load='1hhq' size='340' side='right'caption='[[1hhq]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='1hhq' size='340' side='right'caption='[[1hhq]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1hhq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dicdi Dicdi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HHQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1hhq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HHQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1npk|1npk]], [[1b4s|1b4s]], [[1b99|1b99]], [[1bux|1bux]], [[1f3f|1f3f]], [[1f6t|1f6t]], [[1kdn|1kdn]], [[1leo|1leo]], [[1lwx|1lwx]], [[1ncl|1ncl]], [[2bef|2bef]], [[1hiy|1hiy]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nucleoside-diphosphate_kinase Nucleoside-diphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.6 2.7.4.6] </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=1hhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hhq OCA], [https://pdbe.org/1hhq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hhq RCSB], [https://www.ebi.ac.uk/pdbsum/1hhq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hhq ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hhq OCA], [http://pdbe.org/1hhq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hhq RCSB], [http://www.ebi.ac.uk/pdbsum/1hhq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hhq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/NDKC_DICDI NDKC_DICDI] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Nucleoside diphosphate kinase|Nucleoside diphosphate kinase]] | + | *[[Nucleoside diphosphate kinase 3D structures|Nucleoside diphosphate kinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Dicdi]] | + | [[Category: Dictyostelium discoideum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nucleoside-diphosphate kinase]]
| + | [[Category: Babolat M]] |
| - | [[Category: Babolat, M]] | + | [[Category: Deville-Bonne D]] |
| - | [[Category: Deville-Bonne, D]] | + | [[Category: Janin J]] |
| - | [[Category: Janin, J]] | + | [[Category: Schneider B]] |
| - | [[Category: Schneider, B]] | + | [[Category: Veron M]] |
| - | [[Category: Veron, M]] | + | [[Category: Xu YW]] |
| - | [[Category: Xu, Y W]] | + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Metabolic role]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
NDKC_DICDI
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
Nucleoside diphosphate (NDP) kinase phosphorylates nucleoside diphosphates with little specificity for the base and the sugar. Although nucleotide analogues used in antiviral therapies are also metabolized to their triphosphate form by NDP kinase, their lack of the 3'-hydroxyl of the ribose, which allows them to be DNA chain terminators, severely impairs the catalytic efficiency of NDP kinase. We have analyzed the kinetics parameters of several mutant NDP kinases modified on residues (Lys16, Tyr56, Asn119) interacting with the gamma-phosphate and/or the 3'-OH of the Mg2+-ATP substrate. We compared the relative contributions of the active-site residues and the substrate 3'-OH for point mutations on Lys16, Tyr56 and Asn119. Analysis of additional data from pH profiles identify the ionization state of these residues in the enzyme active form. X-ray structure of K16A mutant NDP kinase shows no detectable rearrangement of the residues of the active site.
Mechanism of phosphoryl transfer by nucleoside diphosphate kinase pH dependence and role of the active site Lys16 and Tyr56 residues.,Schneider B, Babolat M, Xu YW, Janin J, Veron M, Deville-Bonne D Eur J Biochem. 2001 Apr;268(7):1964-71. PMID:11277918[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schneider B, Babolat M, Xu YW, Janin J, Veron M, Deville-Bonne D. Mechanism of phosphoryl transfer by nucleoside diphosphate kinase pH dependence and role of the active site Lys16 and Tyr56 residues. Eur J Biochem. 2001 Apr;268(7):1964-71. PMID:11277918
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