1psd

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[[Image:1psd.gif|left|200px]]
[[Image:1psd.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1psd |SIZE=350|CAPTION= <scene name='initialview01'>1psd</scene>, resolution 2.75&Aring;
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The line below this paragraph, containing "STRUCTURE_1psd", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1psd| PDB=1psd | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1psd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1psd OCA], [http://www.ebi.ac.uk/pdbsum/1psd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1psd RCSB]</span>
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}}
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'''THE ALLOSTERIC LIGAND SITE IN THE VMAX-TYPE COOPERATIVE ENZYME PHOSPHOGLYCERATE DEHYDROGENASE'''
'''THE ALLOSTERIC LIGAND SITE IN THE VMAX-TYPE COOPERATIVE ENZYME PHOSPHOGLYCERATE DEHYDROGENASE'''
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[[Category: Grant, G A.]]
[[Category: Grant, G A.]]
[[Category: Schuller, D J.]]
[[Category: Schuller, D J.]]
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[[Category: oxidoreductase (nad(a))]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:26:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:03:54 2008''
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Revision as of 02:26, 3 May 2008

Image:1psd.gif

Template:STRUCTURE 1psd

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. 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 Page seeded by OCA on Sat May 3 05:26:05 2008

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