|
|
| (2 intermediate revisions not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='1nsp' size='340' side='right'caption='[[1nsp]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='1nsp' size='340' side='right'caption='[[1nsp]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1nsp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NSP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NSP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1nsp]] 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=1NSP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NSP FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIP:ND1-PHOSPHONOHISTIDINE'>HIP</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='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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HIP:ND1-PHOSPHONOHISTIDINE'>HIP</scene></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=1nsp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nsp OCA], [http://pdbe.org/1nsp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nsp RCSB], [http://www.ebi.ac.uk/pdbsum/1nsp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nsp 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=1nsp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nsp OCA], [https://pdbe.org/1nsp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nsp RCSB], [https://www.ebi.ac.uk/pdbsum/1nsp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nsp 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]] |
| Line 34: |
Line 36: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 11735]] | + | [[Category: Dictyostelium discoideum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nucleoside-diphosphate kinase]]
| + | [[Category: Chiadmi M]] |
| - | [[Category: Chiadmi, M]] | + | [[Category: Janin J]] |
| - | [[Category: Janin, J]] | + | [[Category: Lascu I]] |
| - | [[Category: Lascu, I]] | + | [[Category: Lebras G]] |
| - | [[Category: Lebras, G]] | + | [[Category: Morera S]] |
| - | [[Category: Morera, S]] | + | |
| - | [[Category: Nucleoside triphosphate: nucleoside diphosphate]]
| + | |
| - | [[Category: Phosphotransferase]]
| + | |
| 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 kinase (NDP kinase) has a ping-pong mechanism with a phosphohistidine intermediate. Crystals of the enzymes from Dictyostelium discoideum and from Drosophila melanogaster were treated with phosphoramidate, and their X-ray structures were determined at 2.1 and 2.2 A resolution, respectively. The atomic models, refined to R factors below 20%, show no conformation change relative to the free proteins. In both enzymes, the active site histidine was phosphorylated on N delta, and it was the only site of phosphorylation. The phosphate group interacts with the hydroxyl group of Tyr56 and with protein-bound water molecules. Its environment is compared with that of phosphohistidines in succinyl-CoA synthetase and in phosphocarrier proteins. The X-ray structures of phosphorylated NDP kinase and of previously determined complexes with nucleoside diphosphates provide a basis for modeling the Michaelis complex with a nucleoside triphosphate, that of the phosphorylated protein with a nucleoside diphosphate, and the transition state of the phosphate transfer reaction in which the gamma-phosphate is pentacoordinated.
Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium.,Morera S, Chiadmi M, LeBras G, Lascu I, Janin J Biochemistry. 1995 Sep 5;34(35):11062-70. PMID:7669763[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Morera S, Chiadmi M, LeBras G, Lascu I, Janin J. Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium. Biochemistry. 1995 Sep 5;34(35):11062-70. PMID:7669763
|
