4icd: Difference between revisions
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==REGULATION OF ISOCITRATE DEHYDROGENASE BY PHOSPHORYLATION INVOLVES NO LONG-RANGE CONFORMATIONAL CHANGE IN THE FREE ENZYME== | ==REGULATION OF ISOCITRATE DEHYDROGENASE BY PHOSPHORYLATION INVOLVES NO LONG-RANGE CONFORMATIONAL CHANGE IN THE FREE ENZYME== | ||
<StructureSection load='4icd' size='340' side='right' caption='[[4icd]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='4icd' size='340' side='right'caption='[[4icd]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4icd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. The September 2010 RCSB PDB [http://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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ICD FirstGlance]. <br> | <table><tr><td colspan='2'>[[4icd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. The September 2010 RCSB PDB [http://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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ICD FirstGlance]. <br> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ic/4icd_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ic/4icd_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4icd" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4icd" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Isocitrate dehydrogenase 3D structures|Isocitrate dehydrogenase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Bacillus coli migula 1895]] | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Isocitrate Dehydrogenase]] | [[Category: Isocitrate Dehydrogenase]] | ||
[[Category: Large Structures]] | |||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
[[Category: Dean, A M]] | [[Category: Dean, A M]] | ||
Revision as of 07:58, 13 February 2020
REGULATION OF ISOCITRATE DEHYDROGENASE BY PHOSPHORYLATION INVOLVES NO LONG-RANGE CONFORMATIONAL CHANGE IN THE FREE ENZYMEREGULATION OF ISOCITRATE DEHYDROGENASE BY PHOSPHORYLATION INVOLVES NO LONG-RANGE CONFORMATIONAL CHANGE IN THE FREE ENZYME
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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