4icd

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{{Seed}}
 
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[[Image:4icd.png|left|200px]]
 
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==REGULATION OF ISOCITRATE DEHYDROGENASE BY PHOSPHORYLATION INVOLVES NO LONG-RANGE CONFORMATIONAL CHANGE IN THE FREE ENZYME==
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The line below this paragraph, containing "STRUCTURE_4icd", creates the "Structure Box" on the page.
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<StructureSection load='4icd' size='340' side='right'caption='[[4icd]], [[Resolution|resolution]] 2.50&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'>[[4icd]] 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=4ICD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ICD 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]] 2.5&#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=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
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{{STRUCTURE_4icd| PDB=4icd | 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=4icd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4icd OCA], [https://pdbe.org/4icd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4icd RCSB], [https://www.ebi.ac.uk/pdbsum/4icd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4icd 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/ic/4icd_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=4icd 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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The structure of the phosphorylated form of isocitrate dehydrogenase from Escherichia coli has been solved and refined to an R-factor of 16.9% at 2.5-A resolution. Comparison with the structure of the dephosphorylated enzyme shows that there are no large scale conformational changes and that small conformational changes are highly localized around the site of phosphorylation at serine 113. Tyrosine 160 rotates by 15 degrees, and there is a local rearrangement of water structure. There is an 0.2-A net movement of loop 230-234, and side chain shifts of 0.2 A root mean square for isoleucine 159 and lysine 199. The lack of large conformational changes, the observation of a possible isocitrate binding site close to serine 113, and the demonstration that the phosphorylated enzyme is unable to bind isocitrate suggest that this enzyme is inactivated by a direct electrostatic interaction between the substrate and the serine phosphate.
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===REGULATION OF ISOCITRATE DEHYDROGENASE BY PHOSPHORYLATION INVOLVES NO LONG-RANGE CONFORMATIONAL CHANGE IN THE FREE ENZYME===
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Regulation of isocitrate dehydrogenase by phosphorylation involves no long-range conformational change in the free enzyme.,Hurley JH, Dean AM, Thorsness PE, Koshland DE Jr, Stroud RM J Biol Chem. 1990 Mar 5;265(7):3599-602. PMID:2406256<ref>PMID:2406256</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 4icd" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_2406256}}, adds the Publication Abstract to the page
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*[[Isocitrate dehydrogenase 3D structures|Isocitrate dehydrogenase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 2406256 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_2406256}}
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__TOC__
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</StructureSection>
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==About this Structure==
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4ICD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ICD OCA].
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==Reference==
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Regulation of isocitrate dehydrogenase by phosphorylation involves no long-range conformational change in the free enzyme., Hurley JH, Dean AM, Thorsness PE, Koshland DE Jr, Stroud RM, J Biol Chem. 1990 Mar 5;265(7):3599-602. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2406256 2406256]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Isocitrate Dehydrogenase]]
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[[Category: Dean, A M.]]
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[[Category: Large Structures]]
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[[Category: Hurley, J H.]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Koshlandjunior, D E.]]
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[[Category: Dean AM]]
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[[Category: Stroud, R M.]]
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[[Category: Hurley JH]]
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[[Category: Thorsness, P E.]]
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[[Category: Koshlandjunior DE]]
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[[Category: Stroud RM]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:41:53 2008''
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[[Category: Thorsness PE]]

Current revision

REGULATION OF ISOCITRATE DEHYDROGENASE BY PHOSPHORYLATION INVOLVES NO LONG-RANGE CONFORMATIONAL CHANGE IN THE FREE ENZYME

PDB ID 4icd

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