1iat
From Proteopedia
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| - | [[Image:1iat.gif|left|200px]] | + | [[Image:1iat.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF HUMAN PHOSPHOGLUCOSE ISOMERASE/NEUROLEUKIN/AUTOCRINE MOTILITY FACTOR/MATURATION FACTOR''' | + | {{Structure |
| + | |PDB= 1iat |SIZE=350|CAPTION= <scene name='initialview01'>1iat</scene>, resolution 1.62Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</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] | ||
| + | |GENE= GPI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF HUMAN PHOSPHOGLUCOSE ISOMERASE/NEUROLEUKIN/AUTOCRINE MOTILITY FACTOR/MATURATION FACTOR''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IAT is a [ | + | 1IAT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAT OCA]. |
==Reference== | ==Reference== | ||
| - | The crystal structure of human phosphoglucose isomerase at 1.6 A resolution: implications for catalytic mechanism, cytokine activity and haemolytic anaemia., Read J, Pearce J, Li X, Muirhead H, Chirgwin J, Davies C, J Mol Biol. 2001 Jun 1;309(2):447-63. PMID:[http:// | + | The crystal structure of human phosphoglucose isomerase at 1.6 A resolution: implications for catalytic mechanism, cytokine activity and haemolytic anaemia., Read J, Pearce J, Li X, Muirhead H, Chirgwin J, Davies C, J Mol Biol. 2001 Jun 1;309(2):447-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11371164 11371164] |
[[Category: Glucose-6-phosphate isomerase]] | [[Category: Glucose-6-phosphate isomerase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: glycolysis enzyme/neurotrophic growth factor/cytokine]] | [[Category: glycolysis enzyme/neurotrophic growth factor/cytokine]] | ||
[[Category: isomerase]] | [[Category: isomerase]] | ||
| - | [[Category: two alpha/beta | + | [[Category: two alpha/beta domain]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:47:49 2008'' |
Revision as of 09:47, 20 March 2008
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| , resolution 1.62Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | GPI (Homo sapiens) | ||||||
| Activity: | Glucose-6-phosphate isomerase, with EC number 5.3.1.9 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HUMAN PHOSPHOGLUCOSE ISOMERASE/NEUROLEUKIN/AUTOCRINE MOTILITY FACTOR/MATURATION FACTOR
Contents |
Overview
Phosphoglucose isomerase (PGI) is a multifunctional protein, which, inside the cell, functions as a housekeeping enzyme of glycolysis and gluconeogenesis and, outside the cell, exerts wholly unrelated cytokine properties. We have determined the structure of human PGI to a resolution of 1.6 A using X-ray crystallography. The structure is highly similar to other PGIs, especially the architecture of the active site. Fortuitous binding of a sulphate molecule from the crystallisation solution has facilitated an accurate description of the substrate phosphate-binding site. Comparison with both native and inhibitor-bound rabbit PGI structures shows that two loops move closer to the active site upon binding inhibitor. Interestingly, the human structure most closely resembles the inhibitor-bound structure, suggesting that binding of the phosphate moiety of the substrate may trigger this conformational change. We suggest a new mechanism for catalysis that uses Glu357 as the base catalyst for the isomerase reaction rather than His388 as proposed previously. The human PGI structure has also provided a detailed framework with which to map mutations associated with non-spherocytic haemolytic anaemia.
Disease
Known diseases associated with this structure: Hemolytic anemia due to glucosephosphate isomerase deficiency OMIM:[172400], Hydrops fetalis, one form OMIM:[172400]
About this Structure
1IAT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The crystal structure of human phosphoglucose isomerase at 1.6 A resolution: implications for catalytic mechanism, cytokine activity and haemolytic anaemia., Read J, Pearce J, Li X, Muirhead H, Chirgwin J, Davies C, J Mol Biol. 2001 Jun 1;309(2):447-63. PMID:11371164
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