4icd
From Proteopedia
(New page: 200px<br /><applet load="4icd" size="450" color="white" frame="true" align="right" spinBox="true" caption="4icd, resolution 2.5Å" /> '''REGULATION OF ISOCITR...) |
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| - | [[Image:4icd.jpg|left|200px]]<br /><applet load="4icd" size=" | + | [[Image:4icd.jpg|left|200px]]<br /><applet load="4icd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="4icd, resolution 2.5Å" /> | caption="4icd, resolution 2.5Å" /> | ||
'''REGULATION OF ISOCITRATE DEHYDROGENASE BY PHOSPHORYLATION INVOLVES NO LONG-RANGE CONFORMATIONAL CHANGE IN THE FREE ENZYME'''<br /> | '''REGULATION OF ISOCITRATE DEHYDROGENASE BY PHOSPHORYLATION INVOLVES NO LONG-RANGE CONFORMATIONAL CHANGE IN THE FREE ENZYME'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the phosphorylated form of isocitrate dehydrogenase from | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 4ICD 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 PO3 as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 4ICD 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=PO3:'>PO3</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=4ICD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Isocitrate dehydrogenase (NADP(+))]] | [[Category: Isocitrate dehydrogenase (NADP(+))]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dean, A | + | [[Category: Dean, A M.]] |
| - | [[Category: Hurley, J | + | [[Category: Hurley, J H.]] |
| - | [[Category: Koshlandjunior, D | + | [[Category: Koshlandjunior, D E.]] |
| - | [[Category: Stroud, R | + | [[Category: Stroud, R M.]] |
| - | [[Category: Thorsness, P | + | [[Category: Thorsness, P E.]] |
[[Category: PO3]] | [[Category: PO3]] | ||
[[Category: oxidoreductase (nad(a)-choh(d))]] | [[Category: oxidoreductase (nad(a)-choh(d))]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:13:39 2008'' |
Revision as of 17:13, 21 February 2008
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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.
About this Structure
4ICD is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Isocitrate dehydrogenase (NADP(+)), with EC number 1.1.1.42 Full crystallographic information is available from OCA.
Reference
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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