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1idd

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(New page: 200px<br /><applet load="1idd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1idd, resolution 2.5&Aring;" /> '''ISOCITRATE DEHYDROGEN...)
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[[Image:1idd.jpg|left|200px]]<br /><applet load="1idd" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1idd, resolution 2.5&Aring;" />
 
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'''ISOCITRATE DEHYDROGENASE Y160F MUTANT APO ENZYME'''<br />
 
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==Overview==
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==ISOCITRATE DEHYDROGENASE Y160F MUTANT APO ENZYME==
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Two site-directed mutants of isocitrate dehydrogenase (IDH) of Escherichia, coli have been studied by site-directed mutagenesis kinetic and structural, studies. Substitution of phenylalanine for tyrosine at position 160, (Y160F) showed 0.4% of the kcat of wild-type with isocitrate as substrate, while the Km for isocitrate remained unchanged. When the postulated, intermediate, oxalosuccinate, was enzymatically decarboxylated, Y160F, showed a higher kcat and a similar Km to the wild type values. The rate of, reduction of oxalosuccinate to isocitrate by the Y160F mutant was greatly, decreased relative to the wild-type. Substitution of methionine for lysine, at position 230 decreased kcat to 1.1% of that of the wild-type and Km, increased by a factor of 500-600. The decarboxylation of oxalosuccinate, was undetectable for the K230M mutant. The structure of the site-directed, mutants of IDH with and without a bound complex of isocitrate and Mg2+ was, solved at 2.5 A resolution and compared by difference mapping against, previously determined enzyme structures. The structural studies show that, (i) the overall protein-folding side chain conformations and active sites, of both mutants are isomorphous with wild-type enzyme, (ii) isocitrate and, magnesium bind to both enzyme mutants with the same relative conformation, and binding interactions as wild-type enzyme, and (iii) the mutated side, chains (Phe 160 and Met 230) are positioned for catalysis in a similar, conformation as that observed for the wild-type enzyme. Hence, the, alteration of the side chain functional groups is directly related to the, loss of enzyme activity. Possible roles of the active site tyrosine and, lysine are discussed.
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<StructureSection load='1idd' size='340' side='right'caption='[[1idd]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1idd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IDD FirstGlance]. <br>
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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]] 2.5&#8491;</td></tr>
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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=1idd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1idd OCA], [https://pdbe.org/1idd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1idd RCSB], [https://www.ebi.ac.uk/pdbsum/1idd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1idd ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IDH_ECOLI IDH_ECOLI]
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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/id/1idd_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=1idd ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1IDD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IDD OCA].
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*[[Isocitrate dehydrogenase 3D structures|Isocitrate dehydrogenase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Mutational analysis of the catalytic residues lysine 230 and tyrosine 160 in the NADP(+)-dependent isocitrate dehydrogenase from Escherichia coli., Lee ME, Dyer DH, Klein OD, Bolduc JM, Stoddard BL, Koshland DE Jr, Biochemistry. 1995 Jan 10;34(1):378-84. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7819221 7819221]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Isocitrate dehydrogenase (NADP(+))]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Bolduc JM]]
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[[Category: Bolduc, J.M.]]
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[[Category: Dyer DH]]
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[[Category: Dyer, D.H.]]
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[[Category: Klein OD]]
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[[Category: Junior, D.E.Koshland.]]
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[[Category: Koshland Junior DE]]
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[[Category: Klein, O.D.]]
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[[Category: Lee ME]]
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[[Category: Lee, M.E.]]
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[[Category: Stoddard BL]]
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[[Category: Stoddard, B.L.]]
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[[Category: oxidoreductase (nad(a)-choh(d))]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:18:32 2007''
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Current revision

ISOCITRATE DEHYDROGENASE Y160F MUTANT APO ENZYME

PDB ID 1idd

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