1sjs | pdb_00001sjs

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Revision as of 17:31, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1sjs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sjs, resolution 2.42Å" /> '''ACCESS TO PHOSPHORY...)
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ACCESS TO PHOSPHORYLATION IN ISOCITRATE DEHYDROGENASE MAY OCCUR BY DOMAIN SHIFTING

File:1sjs.gif


1sjs, resolution 2.42Å

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Overview

To clarify further the mechanism of regulation by phosphorylation of, isocitrate dehydrogenase, cocrystallization of isocitrate dehydrogenase, and isocitrate dehydrogenase kinase/phosphatase in the presence of an ATP, analog was attempted. Although cocrystallization was unsuccessful, a new, crystal form of isocitrate dehydrogenase was obtained which provides, insight into the phosphorylation mechanism. The new, orthorhombic crystal, form of isocitrate dehydrogenase is related to the previously reported, tetragonal form largely by an approximately 16 degrees shift of a large, domain relative to the small domain and clasp region within each subunit, of the dimeric enzyme. The NADP+ cofactor binding surface is significantly, disrupted by the shift to the open conformation. The ... [(full description)]

About this Structure

1SJS is a [Single protein] structure of sequence from [Escherichia coli]. Active as [[1]], with EC number [1.1.1.42]. Full crystallographic information is available from [OCA].

Reference

Access to phosphorylation in isocitrate dehydrogenase may occur by domain shifting., Finer-Moore J, Tsutakawa SE, Cherbavaz DR, LaPorte DC, Koshland DE Jr, Stroud RM, Biochemistry. 1997 Nov 11;36(45):13890-6. PMID:9374867

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