4icd: Difference between revisions

Revision as of 13:41, 3 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:4icd.png

Template:STRUCTURE 4icd

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

Template:ABSTRACT PUBMED 2406256

About this StructureAbout this Structure

4ICD is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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 {{STRUCTURE_4icd|  PDB=4icd  |  SCENE=  }}
-'''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===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_2406256}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_2406256}}
 ==About this Structure==
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 [[Category: Stroud, R M.]]
 [[Category: Thorsness, P E.]]
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