4icd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:4icd.jpg|left|200px]]<br /><applet load="4icd" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:4icd.jpg|left|200px]]
-
caption="4icd, resolution 2.5&Aring;" />
+
 
-
'''REGULATION OF ISOCITRATE DEHYDROGENASE BY PHOSPHORYLATION INVOLVES NO LONG-RANGE CONFORMATIONAL CHANGE IN THE FREE ENZYME'''<br />
+
{{Structure
 +
|PDB= 4icd |SIZE=350|CAPTION= <scene name='initialview01'>4icd</scene>, resolution 2.5&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=PO3:PHOSPHITE ION'>PO3</scene>
 +
|ACTIVITY= [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]
 +
|GENE=
 +
}}
 +
 
 +
'''REGULATION OF ISOCITRATE DEHYDROGENASE BY PHOSPHORYLATION INVOLVES NO LONG-RANGE CONFORMATIONAL CHANGE IN THE FREE ENZYME'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==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 <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].
+
4ICD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ICD OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2406256 2406256]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/2406256 2406256]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Isocitrate dehydrogenase (NADP(+))]]
[[Category: Isocitrate dehydrogenase (NADP(+))]]
Line 22: Line 31:
[[Category: oxidoreductase (nad(a)-choh(d))]]
[[Category: oxidoreductase (nad(a)-choh(d))]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:13:39 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:10:04 2008''

Revision as of 17:10, 20 March 2008


PDB ID 4icd

Drag the structure with the mouse to rotate
, resolution 2.5Å
Ligands:
Activity: Isocitrate dehydrogenase (NADP(+)), with EC number 1.1.1.42
Coordinates: save as pdb, mmCIF, xml



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. 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

Page seeded by OCA on Thu Mar 20 19:10:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools