1hlw: Difference between revisions

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 <StructureSection load='1hlw' size='340' side='right'caption='[[1hlw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hlw]] 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=1HLW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HLW FirstGlance]. <br>
+<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>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b4s|1b4s]]</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]] 1.9&#8491;</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=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>
-<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=1hlw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hlw OCA], [http://pdbe.org/1hlw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hlw RCSB], [http://www.ebi.ac.uk/pdbsum/1hlw PDBsum], [http://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]]
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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=1hlw ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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:11148034<ref>PMID:11148034</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1hlw" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Nucleoside diphosphate kinase|Nucleoside diphosphate kinase]]
+*[[Nucleoside diphosphate kinase 3D structures|Nucleoside diphosphate kinase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 11735]]
+[[Category: Dictyostelium discoideum]]
 [[Category: Large Structures]]
-[[Category: Nucleoside-diphosphate kinase]]
+[[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]]
-[[Category: Kinase]]
-[[Category: Phosphotransferase]]
-[[Category: Transferase]]