1c7r: Difference between revisions
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|PDB= 1c7r |SIZE=350|CAPTION= <scene name='initialview01'>1c7r</scene>, resolution 2.5Å | |PDB= 1c7r |SIZE=350|CAPTION= <scene name='initialview01'>1c7r</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=PA5:5-PHOSPHOARABINONIC ACID'>PA5</scene> | |LIGAND= <scene name='pdbligand=PA5:5-PHOSPHOARABINONIC+ACID'>PA5</scene> | ||
|ACTIVITY= [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] | |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> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1c7q|1C7Q]] | |||
|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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[[Category: Meng, M.]] | [[Category: Meng, M.]] | ||
[[Category: Sun, Y J.]] | [[Category: Sun, Y J.]] | ||
[[Category: phosphoglucose isomerase/autocrine motility factor/ neuroleukin]] | [[Category: phosphoglucose isomerase/autocrine motility factor/ neuroleukin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:16:17 2008'' | ||
Revision as of 19:16, 30 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Glucose-6-phosphate isomerase, with EC number 5.3.1.9 | ||||||
| Related: | 1C7Q
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF PHOSPHOGLUCOSE ISOMERASE/AUTOCRINE MOTILITY FACTOR/NEUROLEUKIN COMPLEXED WITH ITS CARBOHYDRATE PHOSPHATE INHIBITORS AND ITS SUBSTRATE RECOGNITION MECHANISM
OverviewOverview
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 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
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