1ai3

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(New page: 200px<br /><applet load="1ai3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ai3, resolution 1.9&Aring;" /> '''ORBITAL STEERING IN T...)
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[[Image:1ai3.gif|left|200px]]<br /><applet load="1ai3" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ai3, resolution 1.9&Aring;" />
 
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'''ORBITAL STEERING IN THE CATALYTIC POWER OF ENZYMES: SMALL STRUCTURAL CHANGES WITH LARGE CATALYTIC CONSEQUENCES'''<br />
 
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==Overview==
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==ORBITAL STEERING IN THE CATALYTIC POWER OF ENZYMES: SMALL STRUCTURAL CHANGES WITH LARGE CATALYTIC CONSEQUENCES==
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Small structural perturbations in the enzyme isocitrate dehydrogenase, (IDH) were made in order to evaluate the contribution of precise substrate, alignment to the catalytic power of an enzyme. The reaction trajectory of, IDH was modified (i) after the adenine moiety of nicotinamide adenine, dinucleotide phosphate was changed to hypoxanthine (the 6-amino was, changed to 6-hydroxyl), and (ii) by replacing Mg2+, which has six, coordinating ligands, with Ca2+, which has eight coordinating ligands., Both changes make large (10(-3) to 10(-5)) changes in the reaction, velocity but only small changes in the orientation of the substrates (both, distance and angle) as revealed by cryocrystallographic trapping of active, IDH complexes. The results provide evidence that orbital overlap produced, by optimal orientation of reacting orbitals plays a major quantitative, role in the catalytic power of enzymes.
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<StructureSection load='1ai3' size='340' side='right'caption='[[1ai3]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ai3]] 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=1AI3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AI3 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]] 1.9&#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=NDO:NICOTINAMIDE-(6-DEAMINO-6-HYDROXY-ADENINE)-DINUCLEOTIDE+PHOSPHATE'>NDO</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=1ai3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ai3 OCA], [https://pdbe.org/1ai3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ai3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ai3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ai3 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/ai/1ai3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ai3 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Small structural perturbations in the enzyme isocitrate dehydrogenase (IDH) were made in order to evaluate the contribution of precise substrate alignment to the catalytic power of an enzyme. The reaction trajectory of IDH was modified (i) after the adenine moiety of nicotinamide adenine dinucleotide phosphate was changed to hypoxanthine (the 6-amino was changed to 6-hydroxyl), and (ii) by replacing Mg2+, which has six coordinating ligands, with Ca2+, which has eight coordinating ligands. Both changes make large (10(-3) to 10(-5)) changes in the reaction velocity but only small changes in the orientation of the substrates (both distance and angle) as revealed by cryocrystallographic trapping of active IDH complexes. The results provide evidence that orbital overlap produced by optimal orientation of reacting orbitals plays a major quantitative role in the catalytic power of enzymes.
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==About this Structure==
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Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences.,Mesecar AD, Stoddard BL, Koshland DE Jr Science. 1997 Jul 11;277(5323):202-6. PMID:9211842<ref>PMID:9211842</ref>
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1AI3 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 NDO and ITM 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=1AI3 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences., Mesecar AD, Stoddard BL, Koshland DE Jr, Science. 1997 Jul 11;277(5323):202-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9211842 9211842]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 1ai3" style="background-color:#fffaf0;"></div>
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[[Category: Isocitrate dehydrogenase (NADP(+))]]
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[[Category: Single protein]]
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[[Category: Junior, D.E.Koshland.]]
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[[Category: Mesecar, A.]]
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[[Category: Stoddard, B.L.]]
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[[Category: ITM]]
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[[Category: NDO]]
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[[Category: glyoxylate bypass]]
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[[Category: nadp]]
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[[Category: oxidoreductase (nad(a)-choh(d))]]
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[[Category: phosphorylation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:52:28 2007''
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==See Also==
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*[[Isocitrate dehydrogenase 3D structures|Isocitrate dehydrogenase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Koshland Junior DE]]
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[[Category: Mesecar A]]
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[[Category: Stoddard BL]]

Current revision

ORBITAL STEERING IN THE CATALYTIC POWER OF ENZYMES: SMALL STRUCTURAL CHANGES WITH LARGE CATALYTIC CONSEQUENCES

PDB ID 1ai3

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