1psd

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[[Image:1psd.gif|left|200px]]
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{{Seed}}
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[[Image:1psd.png|left|200px]]
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{{STRUCTURE_1psd| PDB=1psd | SCENE= }}
{{STRUCTURE_1psd| PDB=1psd | SCENE= }}
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'''THE ALLOSTERIC LIGAND SITE IN THE VMAX-TYPE COOPERATIVE ENZYME PHOSPHOGLYCERATE DEHYDROGENASE'''
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===THE ALLOSTERIC LIGAND SITE IN THE VMAX-TYPE COOPERATIVE ENZYME PHOSPHOGLYCERATE DEHYDROGENASE===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 7719856 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7719856}}
==About this Structure==
==About this Structure==
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[[Category: Grant, G A.]]
[[Category: Grant, G A.]]
[[Category: Schuller, D J.]]
[[Category: Schuller, D J.]]
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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 Mon Jul 28 21:13:33 2008''

Revision as of 18:13, 28 July 2008

Image:1psd.png

Template:STRUCTURE 1psd

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

Template:ABSTRACT PUBMED 7719856

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

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