1c7r

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[[Image:1c7r.gif|left|200px]]
[[Image:1c7r.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1c7r |SIZE=350|CAPTION= <scene name='initialview01'>1c7r</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1c7r", 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=PA5:5-PHOSPHOARABINONIC+ACID'>PA5</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/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] </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_1c7r| PDB=1c7r | SCENE= }}
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|RELATEDENTRY=[[1c7q|1C7Q]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c7r OCA], [http://www.ebi.ac.uk/pdbsum/1c7r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c7r RCSB]</span>
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}}
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'''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'''
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[[Category: Meng, M.]]
[[Category: Meng, M.]]
[[Category: Sun, Y J.]]
[[Category: Sun, Y J.]]
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[[Category: phosphoglucose isomerase/autocrine motility factor/ neuroleukin]]
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[[Category: Phosphoglucose isomerase/autocrine motility factor/ neuroleukin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:25:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:16:17 2008''
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Revision as of 09:25, 2 May 2008

Template:STRUCTURE 1c7r

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.

About this Structure

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

Reference

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 Fri May 2 12:25:53 2008

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