1ide

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1ide" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ide, resolution 2.5&Aring;" /> '''ISOCITRATE DEHYDROGEN...)
Line 1: Line 1:
-
[[Image:1ide.jpg|left|200px]]<br /><applet load="1ide" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ide.jpg|left|200px]]<br /><applet load="1ide" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ide, resolution 2.5&Aring;" />
caption="1ide, resolution 2.5&Aring;" />
'''ISOCITRATE DEHYDROGENASE Y160F MUTANT STEADY-STATE INTERMEDIATE COMPLEX (LAUE DETERMINATION)'''<br />
'''ISOCITRATE DEHYDROGENASE Y160F MUTANT STEADY-STATE INTERMEDIATE COMPLEX (LAUE DETERMINATION)'''<br />
==Overview==
==Overview==
-
Site-directed mutagenesis and Laue diffraction data to 2.5 A resolution, were used to solve the structures of two sequential intermediates formed, during the catalytic actions of isocitrate dehydrogenase. Both, intermediates are distinct from the enzyme-substrate and enzyme-product, complexes. Mutation of key catalytic residues changed the rate determining, steps so that protein and substrate intermediates within the overall, reaction pathway could be visualized.
+
Site-directed mutagenesis and Laue diffraction data to 2.5 A resolution were used to solve the structures of two sequential intermediates formed during the catalytic actions of isocitrate dehydrogenase. Both intermediates are distinct from the enzyme-substrate and enzyme-product complexes. Mutation of key catalytic residues changed the rate determining steps so that protein and substrate intermediates within the overall reaction pathway could be visualized.
==About this Structure==
==About this Structure==
-
1IDE 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 MG, ICT and NAP as [http://en.wikipedia.org/wiki/ligands ligands]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IDE OCA].
+
1IDE 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=MG:'>MG</scene>, <scene name='pdbligand=ICT:'>ICT</scene> and <scene name='pdbligand=NAP:'>NAP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1IDE OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Isocitrate dehydrogenase (NADP(+))]]
[[Category: Isocitrate dehydrogenase (NADP(+))]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Bolduc, J.M.]]
+
[[Category: Bolduc, J M.]]
-
[[Category: Dyer, D.H.]]
+
[[Category: Dyer, D H.]]
-
[[Category: Junior, D.E.Koshland.]]
+
[[Category: Junior, D E.Koshland.]]
-
[[Category: Scott, W.G.]]
+
[[Category: Scott, W G.]]
[[Category: Singer, P.]]
[[Category: Singer, P.]]
-
[[Category: Stoddard, B.L.]]
+
[[Category: Stoddard, B L.]]
-
[[Category: Sweet, R.M.]]
+
[[Category: Sweet, R M.]]
[[Category: ICT]]
[[Category: ICT]]
[[Category: MG]]
[[Category: MG]]
Line 26: Line 26:
[[Category: oxidoreductase (nad(a)-choh(d))]]
[[Category: oxidoreductase (nad(a)-choh(d))]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:18:37 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:10:42 2008''

Revision as of 11:10, 21 February 2008


1ide, resolution 2.5Å

Drag the structure with the mouse to rotate

ISOCITRATE DEHYDROGENASE Y160F MUTANT STEADY-STATE INTERMEDIATE COMPLEX (LAUE DETERMINATION)

Overview

Site-directed mutagenesis and Laue diffraction data to 2.5 A resolution were used to solve the structures of two sequential intermediates formed during the catalytic actions of isocitrate dehydrogenase. Both intermediates are distinct from the enzyme-substrate and enzyme-product complexes. Mutation of key catalytic residues changed the rate determining steps so that protein and substrate intermediates within the overall reaction pathway could be visualized.

About this Structure

1IDE is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as Isocitrate dehydrogenase (NADP(+)), with EC number 1.1.1.42 Full crystallographic information is available from OCA.

Reference

Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase., Bolduc JM, Dyer DH, Scott WG, Singer P, Sweet RM, Koshland DE Jr, Stoddard BL, Science. 1995 Jun 2;268(5215):1312-8. PMID:7761851

Page seeded by OCA on Thu Feb 21 13:10:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools