1psd

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(New page: 200px<br /><applet load="1psd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1psd, resolution 2.75&Aring;" /> '''THE ALLOSTERIC LIGAN...)
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[[Image:1psd.gif|left|200px]]<br /><applet load="1psd" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1psd, resolution 2.75&Aring;" />
caption="1psd, resolution 2.75&Aring;" />
'''THE ALLOSTERIC LIGAND SITE IN THE VMAX-TYPE COOPERATIVE ENZYME PHOSPHOGLYCERATE DEHYDROGENASE'''<br />
'''THE ALLOSTERIC LIGAND SITE IN THE VMAX-TYPE COOPERATIVE ENZYME PHOSPHOGLYCERATE DEHYDROGENASE'''<br />
==Overview==
==Overview==
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The crystal structure of the phosphoglycerate dehydrogenase from, Escherichia coli is unique among dehydrogenases. It consists of three, clearly separate domains connected by flexible hinges. The tetramer has, approximate 222 symmetry with the principal contacts between the subunits, forming between either the nucleotide binding domains or the regulatory, domains. Two slightly different subunit conformations are present which, vary only in the orientations of the domains. There is a hinge-like, arrangement near the active site cleft and the serine effector site is, provided by the regulatory domain of each of two subunits. Interdomain, flexibility may play a key role in both catalysis and allosteric, inhibition.
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The crystal structure of the phosphoglycerate dehydrogenase from Escherichia coli is unique among dehydrogenases. It consists of three clearly separate domains connected by flexible hinges. The tetramer has approximate 222 symmetry with the principal contacts between the subunits forming between either the nucleotide binding domains or the regulatory domains. Two slightly different subunit conformations are present which vary only in the orientations of the domains. There is a hinge-like arrangement near the active site cleft and the serine effector site is provided by the regulatory domain of each of two subunits. Interdomain flexibility may play a key role in both catalysis and allosteric inhibition.
==About this Structure==
==About this Structure==
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1PSD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k12 Escherichia coli k12] with NAD and SER as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_dehydrogenase Phosphoglycerate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.95 1.1.1.95] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PSD OCA].
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1PSD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k12 Escherichia coli k12] with <scene name='pdbligand=NAD:'>NAD</scene> and <scene name='pdbligand=SER:'>SER</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_dehydrogenase Phosphoglycerate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.95 1.1.1.95] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PSD OCA].
==Reference==
==Reference==
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[[Category: Phosphoglycerate dehydrogenase]]
[[Category: Phosphoglycerate dehydrogenase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Banaszak, L.J.]]
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[[Category: Banaszak, L J.]]
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[[Category: Grant, G.A.]]
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[[Category: Grant, G A.]]
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[[Category: Schuller, D.J.]]
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[[Category: Schuller, D J.]]
[[Category: NAD]]
[[Category: NAD]]
[[Category: SER]]
[[Category: SER]]
[[Category: oxidoreductase (nad(a))]]
[[Category: oxidoreductase (nad(a))]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:05:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:03 2008''

Revision as of 12:32, 21 February 2008


1psd, resolution 2.75Å

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THE ALLOSTERIC LIGAND SITE IN THE VMAX-TYPE COOPERATIVE ENZYME PHOSPHOGLYCERATE DEHYDROGENASE

Overview

The crystal structure of the phosphoglycerate dehydrogenase from Escherichia coli is unique among dehydrogenases. It consists of three clearly separate domains connected by flexible hinges. The tetramer has approximate 222 symmetry with the principal contacts between the subunits forming between either the nucleotide binding domains or the regulatory domains. Two slightly different subunit conformations are present which vary only in the orientations of the domains. There is a hinge-like arrangement near the active site cleft and the serine effector site is provided by the regulatory domain of each of two subunits. Interdomain flexibility may play a key role in both catalysis and allosteric inhibition.

About this Structure

1PSD is a Single protein structure of sequence from Escherichia coli k12 with and as ligands. Active as Phosphoglycerate dehydrogenase, with EC number 1.1.1.95 Full crystallographic information is available from OCA.

Reference

The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase., Schuller DJ, Grant GA, Banaszak LJ, Nat Struct Biol. 1995 Jan;2(1):69-76. PMID:7719856

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