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1ide

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(New page: 200px<br /><applet load="1ide" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ide, resolution 2.5&Aring;" /> '''ISOCITRATE DEHYDROGEN...)
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[[Image:1ide.jpg|left|200px]]<br /><applet load="1ide" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ide, resolution 2.5&Aring;" />
 
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'''ISOCITRATE DEHYDROGENASE Y160F MUTANT STEADY-STATE INTERMEDIATE COMPLEX (LAUE DETERMINATION)'''<br />
 
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==Overview==
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==ISOCITRATE DEHYDROGENASE Y160F MUTANT STEADY-STATE INTERMEDIATE COMPLEX (LAUE DETERMINATION)==
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Site-directed mutagenesis and Laue diffraction data to 2.5 A resolution, were used to solve the structures of two sequential intermediates formed, during the catalytic actions of isocitrate dehydrogenase. Both, intermediates are distinct from the enzyme-substrate and enzyme-product, complexes. Mutation of key catalytic residues changed the rate determining, steps so that protein and substrate intermediates within the overall, reaction pathway could be visualized.
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<StructureSection load='1ide' size='340' side='right'caption='[[1ide]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ide]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The September 2010 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Isocitrate Dehydrogenase'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2010_9 10.2210/rcsb_pdb/mom_2010_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IDE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IDE 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ICT:ISOCITRIC+ACID'>ICT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></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=1ide FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ide OCA], [https://pdbe.org/1ide PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ide RCSB], [https://www.ebi.ac.uk/pdbsum/1ide PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ide 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/1ide_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=1ide 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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1IDE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG, ICT and NAP as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1IDE 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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Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase., Bolduc JM, Dyer DH, Scott WG, Singer P, Sweet RM, Koshland DE Jr, Stoddard BL, Science. 1995 Jun 2;268(5215):1312-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7761851 7761851]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Isocitrate dehydrogenase (NADP(+))]]
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[[Category: Isocitrate Dehydrogenase]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bolduc, J.M.]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Dyer, D.H.]]
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[[Category: Bolduc JM]]
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[[Category: Junior, D.E.Koshland.]]
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[[Category: Dyer DH]]
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[[Category: Scott, W.G.]]
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[[Category: Koshland Junior DE]]
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[[Category: Singer, P.]]
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[[Category: Scott WG]]
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[[Category: Stoddard, B.L.]]
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[[Category: Singer P]]
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[[Category: Sweet, R.M.]]
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[[Category: Stoddard BL]]
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[[Category: ICT]]
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[[Category: Sweet RM]]
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[[Category: MG]]
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[[Category: NAP]]
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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 17:18:37 2007''
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ISOCITRATE DEHYDROGENASE Y160F MUTANT STEADY-STATE INTERMEDIATE COMPLEX (LAUE DETERMINATION)

PDB ID 1ide

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