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| [[Image:1ncl.jpg|left|200px]]
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| {{Structure
| | ==THERMAL STABILITY OF HEXAMERIC AND TETRAMERIC NUCLEOSIDE, DIPHOSPHATE KINASES== |
| |PDB= 1ncl |SIZE=350|CAPTION= <scene name='initialview01'>1ncl</scene>, resolution 2.2Å
| | <StructureSection load='1ncl' size='340' side='right'caption='[[1ncl]], [[Resolution|resolution]] 2.20Å' scene=''> |
| |SITE=
| | == Structural highlights == |
| |LIGAND=
| | <table><tr><td colspan='2'>[[1ncl]] 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=1NCL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NCL FirstGlance]. <br> |
| |ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| |GENE= | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ncl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ncl OCA], [https://pdbe.org/1ncl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ncl RCSB], [https://www.ebi.ac.uk/pdbsum/1ncl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ncl ProSAT]</span></td></tr> |
| |DOMAIN=
| | </table> |
| |RELATEDENTRY=
| | == Function == |
| |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ncl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ncl OCA], [http://www.ebi.ac.uk/pdbsum/1ncl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ncl RCSB]</span>
| | [https://www.uniprot.org/uniprot/NDKC_DICDI NDKC_DICDI] |
| }}
| | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> |
| | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nc/1ncl_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> |
| | </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=1ncl ConSurf]. |
| | <div style="clear:both"></div> |
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| '''THERMAL STABILITY OF HEXAMERIC AND TETRAMERIC NUCLEOSIDE, DIPHOSPHATE KINASES'''
| | ==See Also== |
| | | *[[Nucleoside diphosphate kinase 3D structures|Nucleoside diphosphate kinase 3D structures]] |
| | | __TOC__ |
| ==Overview== | | </StructureSection> |
| The eukaryotic nucleoside diphosphate (NDP) kinases are hexamers, while the bacterial NDP kinases are tetramers made of small, single domain subunits. These enzymes represent an ideal model for studying the effect of subunit interaction on protein stability. The thermostability of NDP kinases of each class was studied by differential scanning calorimetry and biochemical methods. The hexameric NDP kinase from Dictyostelium discoideum displays one single, irreversible differential scanning calorimetry peak (Tm 62 degrees C) over a broad protein concentration, indicating a single step denaturation. The thermal stability of the protein was increased by ADP. The P105G substitution, which affects a loop implicated in subunit contacts, yields a protein that reversibly dissociates to folded monomers at 38 degrees C before the irreversible denaturation occurs (Tm 47 degrees C). ADP delays the dissociation, but does not change the Tm. These data indicate a "coupling" of the quaternary structure with the tertiary structure in the wild-type, but not in the mutated protein. We describe the x-ray structure of the P105G mutant at 2.2-A resolution. It is very similar to that of the wild-type protein. Therefore, a minimal change in the structure leads to a dramatic change of protein thermostability. The NDP kinase from Escherichia coli behaves like the P105G mutant of the Dictyostelium NDP kinase. The detailed study of their thermostability is important, since biological effects of thermolabile NDP kinases have been described in several organisms.
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| ==About this Structure==
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| 1NCL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NCL OCA].
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| ==Reference==
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| Thermal stability of hexameric and tetrameric nucleoside diphosphate kinases. Effect of subunit interaction., Giartosio A, Erent M, Cervoni L, Morera S, Janin J, Konrad M, Lascu I, J Biol Chem. 1996 Jul 26;271(30):17845-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8663370 8663370]
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| [[Category: Dictyostelium discoideum]] | | [[Category: Dictyostelium discoideum]] |
| [[Category: Nucleoside-diphosphate kinase]] | | [[Category: Large Structures]] |
| [[Category: Single protein]]
| | [[Category: Janin J]] |
| [[Category: Janin, J.]] | | [[Category: Lascu I]] |
| [[Category: Lascu, I.]] | | [[Category: Morera S]] |
| [[Category: Morera, S.]] | |
| [[Category: atp-binding]]
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| [[Category: enzyme]]
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| [[Category: kinase]]
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| [[Category: transferase]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:28:33 2008''
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