1idc

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(New page: 200px<br /><applet load="1idc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1idc, resolution 2.5&Aring;" /> '''ISOCITRATE DEHYDROGEN...)
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[[Image:1idc.jpg|left|200px]]<br /><applet load="1idc" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1idc.jpg|left|200px]]<br /><applet load="1idc" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1idc, resolution 2.5&Aring;" />
caption="1idc, resolution 2.5&Aring;" />
'''ISOCITRATE DEHYDROGENASE FROM E.COLI (MUTANT K230M), STEADY-STATE INTERMEDIATE COMPLEX DETERMINED BY LAUE CRYSTALLOGRAPHY'''<br />
'''ISOCITRATE DEHYDROGENASE FROM E.COLI (MUTANT K230M), STEADY-STATE INTERMEDIATE COMPLEX DETERMINED BY LAUE CRYSTALLOGRAPHY'''<br />
==Overview==
==Overview==
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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.
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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==
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1IDC 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 and OXS 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=1IDC OCA].
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1IDC 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> and <scene name='pdbligand=OXS:'>OXS</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=1IDC OCA].
==Reference==
==Reference==
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[[Category: Isocitrate dehydrogenase (NADP(+))]]
[[Category: Isocitrate dehydrogenase (NADP(+))]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bolduc, J.M.]]
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[[Category: Bolduc, J M.]]
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[[Category: Dyer, D.H.]]
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[[Category: Dyer, D H.]]
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[[Category: Junior, D.E.Koshland.]]
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[[Category: Junior, D E.Koshland.]]
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[[Category: Scott, W.G.]]
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[[Category: Scott, W G.]]
[[Category: Singer, P.]]
[[Category: Singer, P.]]
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[[Category: Stoddard, B.L.]]
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[[Category: Stoddard, B L.]]
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[[Category: Sweet, R.M.]]
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[[Category: Sweet, R M.]]
[[Category: MG]]
[[Category: MG]]
[[Category: OXS]]
[[Category: OXS]]
[[Category: oxidoreductase (nad(a)-choh(d))]]
[[Category: oxidoreductase (nad(a)-choh(d))]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:18:27 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:10:43 2008''

Revision as of 11:10, 21 February 2008


1idc, resolution 2.5Å

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ISOCITRATE DEHYDROGENASE FROM E.COLI (MUTANT K230M), STEADY-STATE INTERMEDIATE COMPLEX DETERMINED BY LAUE CRYSTALLOGRAPHY

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

1IDC 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 13:10:43 2008

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