3aky

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[[Image:3aky.jpg|left|200px]]
 
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==STABILITY, ACTIVITY AND STRUCTURE OF ADENYLATE KINASE MUTANTS==
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The line below this paragraph, containing "STRUCTURE_3aky", creates the "Structure Box" on the page.
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<StructureSection load='3aky' size='340' side='right'caption='[[3aky]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3aky]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AKY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AKY FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.23&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AP5:BIS(ADENOSINE)-5-PENTAPHOSPHATE'>AP5</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>
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{{STRUCTURE_3aky| PDB=3aky | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3aky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aky OCA], [https://pdbe.org/3aky PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aky RCSB], [https://www.ebi.ac.uk/pdbsum/3aky PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aky ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KAD2_YEAST KAD2_YEAST] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.[HAMAP-Rule:MF_03168]<ref>PMID:18433446</ref> <ref>PMID:2848829</ref> <ref>PMID:2850178</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ak/3aky_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=3aky ConSurf].
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<div style="clear:both"></div>
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'''STABILITY, ACTIVITY AND STRUCTURE OF ADENYLATE KINASE MUTANTS'''
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==See Also==
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*[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]]
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== References ==
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==Overview==
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<references/>
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Sequence/structure relationships have been explored by site-directed mutagenesis using a structurally known adenylate kinase. In particular the effects of helix capping and nonpolar core expansion on thermodynamic stability have been analyzed. Six point mutations were produced and characterized by SDS/PAGE, native PAGE, isoelectric focussing, electrophoretic titration, enzyme kinetics, and X-ray structure analysis. Heat-denaturation experiments yielded melting temperatures Tm and melting enthalpy changes delta Hm. The heat capacity change delta Cp of the wild-type enzyme was determined by guanidine hydrochloride denaturation in conjunction with Tm and delta Hm. Using the wild-type delta Cp value, Gibbs free energy changes delta G at room temperature were calculated for all mutants. Four mutants were designed for helix capping stabilization, but only one of them showed such an effect. Because of electrostatic interference with the induced-fit motion, one mutant decreased the catalytic activity strongly. Two mutants expanded nonpolar cores causing destabilization. The mutant with the lower stability could be crystallized and subjected to an X-ray analysis at 223-pm resolution which showed the structural changes. The enzyme was stabilized by adding a -Pro-His-His tail to the C-terminal alpha-helix for nickel-chelate chromatography. This addition constitutes a helix cap. Taken together, the results demonstrate that stabilization by helix capping is difficult to achieve because the small positive effect is drowned by adverse mutational disruption. Further addition of atoms to nonpolar cores destabilized the protein, although the involved geometry changes were very small, demonstrating the importance of efficient packing.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3AKY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AKY OCA].
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==Reference==
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Stability, activity and structure of adenylate kinase mutants., Spuergin P, Abele U, Schulz GE, Eur J Biochem. 1995 Jul 15;231(2):405-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7635152 7635152]
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[[Category: Adenylate kinase]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Abele U]]
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[[Category: Abele, U.]]
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[[Category: Schulz GE]]
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[[Category: Schulz, G E.]]
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[[Category: Atp:amp phosphotransferase]]
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[[Category: Myokinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:19:14 2008''
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Current revision

STABILITY, ACTIVITY AND STRUCTURE OF ADENYLATE KINASE MUTANTS

PDB ID 3aky

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