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[[Image:8icd.gif|left|200px]]<br /><applet load="8icd" size="350" color="white" frame="true" align="right" spinBox="true"
caption="8icd, resolution 2.5&Aring;" />
'''REGULATION OF AN ENZYME BY PHOSPHORYLATION AT THE ACTIVE SITE'''<br />


==Overview==
==REGULATION OF AN ENZYME BY PHOSPHORYLATION AT THE ACTIVE SITE==
The isocitrate dehydrogenase of Escherichia coli is an example of a ubiquitous class of enzymes that are regulated by covalent modification. In the three-dimensional structure of the enzyme-substrate complex, isocitrate forms a hydrogen bond with Ser113, the site of regulatory phosphorylation. The structures of Asp113 and Glu113 mutants, which mimic the inactivation of the enzyme by phosphorylation, show minimal conformational changes from wild type, as in the phosphorylated enzyme. Calculations based on observed structures suggest that the change in electrostatic potential when a negative charge is introduced either by phosporylation or site-directed mutagenesis is sufficient to inactivate the enzyme. Thus, direct interaction at a ligand binding site is an alternative mechanism to induced conformational changes from an allosteric site in the regulation of protein activity by phosphorylation.
<StructureSection load='8icd' size='340' side='right'caption='[[8icd]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8icd]] 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=8ICD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ICD FirstGlance]. <br>
</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>
<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></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8icd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8icd OCA], [https://pdbe.org/8icd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8icd RCSB], [https://www.ebi.ac.uk/pdbsum/8icd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8icd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IDH_ECOLI IDH_ECOLI]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ic/8icd_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=8icd ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
8ICD 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 <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ICT:'>ICT</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=8ICD OCA].
*[[Isocitrate dehydrogenase 3D structures|Isocitrate dehydrogenase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Regulation of an enzyme by phosphorylation at the active site., Hurley JH, Dean AM, Sohl JL, Koshland DE Jr, Stroud RM, Science. 1990 Aug 31;249(4972):1012-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2204109 2204109]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Isocitrate dehydrogenase (NADP(+))]]
[[Category: Isocitrate Dehydrogenase]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Dean, A M.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Hurley, J H.]]
[[Category: Dean AM]]
[[Category: Koshlandjunior, D E.]]
[[Category: Hurley JH]]
[[Category: Sohl, J L.]]
[[Category: Koshlandjunior DE]]
[[Category: Stroud, R M.]]
[[Category: Sohl JL]]
[[Category: ICT]]
[[Category: Stroud RM]]
[[Category: MG]]
[[Category: oxidoreductase (nad(a)-choh(d))]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:17:57 2008''

Latest revision as of 12:42, 14 February 2024

REGULATION OF AN ENZYME BY PHOSPHORYLATION AT THE ACTIVE SITEREGULATION OF AN ENZYME BY PHOSPHORYLATION AT THE ACTIVE SITE

Structural highlights

8icd is a 1 chain structure with sequence from Escherichia coli. The September 2010 RCSB PDB Molecule of the Month feature on Isocitrate Dehydrogenase by David Goodsell is 10.2210/rcsb_pdb/mom_2010_9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IDH_ECOLI

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

8icd, resolution 2.50Å

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