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| [[Image:1hlw.jpg|left|200px]]
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| {{Structure
| | ==STRUCTURE OF THE H122A MUTANT OF THE NUCLEOSIDE DIPHOSPHATE KINASE== |
| |PDB= 1hlw |SIZE=350|CAPTION= <scene name='initialview01'>1hlw</scene>, resolution 1.90Å
| | <StructureSection load='1hlw' size='340' side='right'caption='[[1hlw]], [[Resolution|resolution]] 1.90Å' scene=''> |
| |SITE=
| | == Structural highlights == |
| |LIGAND=
| | <table><tr><td colspan='2'>[[1hlw]] 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=1HLW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HLW FirstGlance]. <br> |
| |ACTIVITY= [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]
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=1hlw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hlw OCA], [https://pdbe.org/1hlw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hlw RCSB], [https://www.ebi.ac.uk/pdbsum/1hlw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hlw ProSAT]</span></td></tr> |
| }}
| | </table> |
| | == Function == |
| | [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/hl/1hlw_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=1hlw ConSurf]. |
| | <div style="clear:both"></div> |
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| '''STRUCTURE OF THE H122A MUTANT OF THE NUCLEOSIDE DIPHOSPHATE KINASE'''
| | ==See Also== |
| | | *[[Nucleoside diphosphate kinase 3D structures|Nucleoside diphosphate kinase 3D structures]] |
| | | __TOC__ |
| ==Overview== | | </StructureSection> |
| We have explored the ability of a nucleoside diphosphate kinase (NDPK) mutant in which the nucleophilic histidine has been replaced by glycine (H122G) to transfer phosphate from ATP to alcohols of varying pK(a), size, shape, and polarity. This cavity mutant does indeed act as a primitive alcohol kinase. The rate of its phosphoryl transfer to alcohols varies considerably, with values spanning a DeltaDeltaG(double dagger) range of 4 kcal/mol, whereas the alcohols have very similar intrinsic reactivities. Analysis of these results suggests that the ability to carry out phosphoryl transfer within the cavity is not a simple function of being small enough to enter the cavity, but rather is a complex function of steric, solvation, entropic, van der Waals packing, and electrostatic properties of the alcohol. In addition, large differences are observed between the reactivities of alcohols within the nucleophile cavity of H122G and the reactivities of the same alcohols within the nucleophile cavity of H122A, a mutant NDPK that differs from H122G by a single methyl group within the cavity. The crystal structures of the two cavity mutants are very similar to one another and to wild-type NDPK, providing no evidence for a structurally perturbed active site. The differences in reactivity between the two mutant proteins illustrate a fundamental limitation of energetic analysis from site-directed mutagenesis: although removal of a side chain is generally considered to be a conservative change, the energetic effects of any given mutation are inextricably linked to the molecular properties of the created cavity and the surrounding protein environment.
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| ==About this Structure==
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| 1HLW 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=1HLW OCA].
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| ==Reference==
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| Chemical rescue of phosphoryl transfer in a cavity mutant: a cautionary tale for site-directed mutagenesis., Admiraal SJ, Meyer P, Schneider B, Deville-Bonne D, Janin J, Herschlag D, Biochemistry. 2001 Jan 16;40(2):403-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11148034 11148034]
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| [[Category: Dictyostelium discoideum]] | | [[Category: Dictyostelium discoideum]] |
| [[Category: Nucleoside-diphosphate kinase]] | | [[Category: Large Structures]] |
| [[Category: Single protein]]
| | [[Category: Admiraal SJ]] |
| [[Category: Admiraal, S J.]] | | [[Category: Deville-Bonne D]] |
| [[Category: Deville-Bonne, D.]] | | [[Category: Herschlag D]] |
| [[Category: Herschlag, D.]] | | [[Category: Janin J]] |
| [[Category: Janin, J.]] | | [[Category: Meyer P]] |
| [[Category: Meyer, P.]] | | [[Category: Schneider B]] |
| [[Category: Schneider, B.]] | |
| [[Category: atp-binding]]
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| [[Category: kinase]]
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| [[Category: phosphotransferase]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:38:55 2008''
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