1n8t: Difference between revisions

Revision as of 17:45, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1n8t.png

Template:STRUCTURE 1n8t

The crystal structure of phosphoglucose isomerase from rabbit muscleThe crystal structure of phosphoglucose isomerase from rabbit muscle

Template:ABSTRACT PUBMED 12595702

About this StructureAbout this Structure

1N8T is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of native phosphoglucose isomerase from rabbit: conformational changes associated with catalytic function., Davies C, Muirhead H, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):453-65. Epub 2003, Feb 21. PMID:12595702

Page seeded by OCA on Sun Jul 27 17:45:38 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''The crystal structure of phosphoglucose isomerase from rabbit muscle'''
+===The crystal structure of phosphoglucose isomerase from rabbit muscle===
-==Overview==
+<!--
-Phosphoglucose isomerase (PGI) is a housekeeping enzyme of metabolism that catalyses the interconversion of glucose 6-phosphate and fructose 6-phosphate, with roles in the glycolytic and gluconeogenic pathways. PGI is also a multifunctional protein that manifests the properties of a cytokine in a wide array of cellular processes, including the production of immunoglobulin by B cells and tumour-cell differentiation. The crystal structure of PGI in the native form from rabbit muscle has been solved at a resolution of 2.5 A by a combination of multiple isomorphous replacement and multi-crystal averaging techniques. Comparison with published structures of rabbit PGI in complex with three inhibitors and with the substrate fructose 6-phosphate reveals a number of conformational changes that may be associated with catalytic function. These occur in the small domain around the sugar phosphate-binding site, in a small helix carrying His388 and in a helix near the C-terminal end. One of these may be the structural rearrangement that has been postulated to be the rate-limiting step for catalysis.
+The line below this paragraph, {{ABSTRACT_PUBMED_12595702}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12595702 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12595702}}
 ==About this Structure==
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 [[Category: Cytokine]]
 [[Category: Glycolysis]]
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