1c7r: Difference between revisions

Revision as of 20:19, 30 June 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:1c7r.png

Template:STRUCTURE 1c7r

THE CRYSTAL STRUCTURE OF PHOSPHOGLUCOSE ISOMERASE/AUTOCRINE MOTILITY FACTOR/NEUROLEUKIN COMPLEXED WITH ITS CARBOHYDRATE PHOSPHATE INHIBITORS AND ITS SUBSTRATE RECOGNITION MECHANISMTHE CRYSTAL STRUCTURE OF PHOSPHOGLUCOSE ISOMERASE/AUTOCRINE MOTILITY FACTOR/NEUROLEUKIN COMPLEXED WITH ITS CARBOHYDRATE PHOSPHATE INHIBITORS AND ITS SUBSTRATE RECOGNITION MECHANISM

Template:ABSTRACT PUBMED 10770936

About this StructureAbout this Structure

1C7R is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of phosphoglucose isomerase/autocrine motility factor/neuroleukin complexed with its carbohydrate phosphate inhibitors suggests its substrate/receptor recognition., Chou CC, Sun YJ, Meng M, Hsiao CD, J Biol Chem. 2000 Jul 28;275(30):23154-60. PMID:10770936

Page seeded by OCA on Mon Jun 30 20:19:58 2008

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OCA

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 {{STRUCTURE_1c7r|  PDB=1c7r  |  SCENE=  }}
-'''THE CRYSTAL STRUCTURE OF PHOSPHOGLUCOSE ISOMERASE/AUTOCRINE MOTILITY FACTOR/NEUROLEUKIN COMPLEXED WITH ITS CARBOHYDRATE PHOSPHATE INHIBITORS AND ITS SUBSTRATE RECOGNITION MECHANISM'''
+===THE CRYSTAL STRUCTURE OF PHOSPHOGLUCOSE ISOMERASE/AUTOCRINE MOTILITY FACTOR/NEUROLEUKIN COMPLEXED WITH ITS CARBOHYDRATE PHOSPHATE INHIBITORS AND ITS SUBSTRATE RECOGNITION MECHANISM===
-==Overview==
+<!--
-Phosphoglucose isomerase catalyzes the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate. In addition, phosphoglucose isomerase has been shown to have functions equivalent to neuroleukin, autocrine motility factor, and maturation factor. Here we present the crystal structures of phosphoglucose isomerase complexed with 5-phospho-D-arabinonate and N-bromoacetylethanolamine phosphate at 2.5- and 2.3-A resolution, respectively. The inhibitors bind to a region within the domains' interface and interact with a histidine residue (His(306)) from the other subunit. We also demonstrated that the inhibitors not only affect the enzymatic activity of phosphoglucose isomerase, but can also inhibit the autocrine motility factor-induced cell motility of CT-26 mouse colon tumor cells. These results indicate that the substrate and the receptor binding sites of phosphoglucose isomerase and autocrine motility factor are located within close proximity to each other. Based on these two complex structures, together with biological and biochemical results, we propose a possible isomerization mechanism for phosphoglucose isomerase.
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+{{ABSTRACT_PUBMED_10770936}}
 ==About this Structure==
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 [[Category: Sun, Y J.]]
 [[Category: Phosphoglucose isomerase/autocrine motility factor/ neuroleukin]]
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