1ai2

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[[Image:1ai2.gif|left|200px]]
 
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{{Structure
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==ISOCITRATE DEHYDROGENASE COMPLEXED WITH ISOCITRATE, NADP+, AND CALCIUM (FLASH-COOLED)==
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|PDB= 1ai2 |SIZE=350|CAPTION= <scene name='initialview01'>1ai2</scene>, resolution 1.9&Aring;
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<StructureSection load='1ai2' size='340' side='right'caption='[[1ai2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene> and <scene name='pdbligand=ICA:ISOCITRATE CALCIUM COMPLEX'>ICA</scene>
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<table><tr><td colspan='2'>[[1ai2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ikb 1ikb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AI2 FirstGlance]. <br>
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|ACTIVITY= [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]
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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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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ICA:ISOCITRATE+CALCIUM+COMPLEX'>ICA</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
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}}
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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=1ai2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ai2 OCA], [https://pdbe.org/1ai2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ai2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ai2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ai2 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/1ai2_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=1ai2 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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'''ISOCITRATE DEHYDROGENASE COMPLEXED WITH ISOCITRATE, NADP+, AND CALCIUM (FLASH-COOLED)'''
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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1ai2" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Isocitrate dehydrogenase 3D structures|Isocitrate dehydrogenase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1AI2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry 1IKB. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AI2 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/9211842 9211842]
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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: Koshland Junior DE]]
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[[Category: Junior, D E.Koshland.]]
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[[Category: Mesecar A]]
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[[Category: Mesecar, A.]]
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[[Category: Stoddard BL]]
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[[Category: Stoddard, B L.]]
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[[Category: ICA]]
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[[Category: NAP]]
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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://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:57:52 2008''
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Current revision

ISOCITRATE DEHYDROGENASE COMPLEXED WITH ISOCITRATE, NADP+, AND CALCIUM (FLASH-COOLED)

PDB ID 1ai2

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