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1nuh

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(New page: 200px<br /> <applet load="1nuh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nuh, resolution 2.51&Aring;" /> '''The crystal structu...)
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'''The crystal structure of human phosphoglucose isomerase complexed with 5-phosphoarabinonate'''<br />
'''The crystal structure of human phosphoglucose isomerase complexed with 5-phosphoarabinonate'''<br />
==Overview==
==Overview==
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Phosphoglucose isomerase (PGI) is a workhorse enzyme of carbohydrate, metabolism that interconverts glucose 6-phosphate and fructose, 6-phosphate. Outside the cell, however, the protein appears to function as, a cytokine. A crystal structure of human PGI bound with, 5-phosphoarabinonate, a strong inhibitor that mimics the cis-enediol(ate), intermediate of the reaction, has been determined at 2.5 A resolution. The, structure helps to confirm the assignment of Glu357 as the base catalyst, in the isomerase reaction.
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Phosphoglucose isomerase (PGI) is a workhorse enzyme of carbohydrate metabolism that interconverts glucose 6-phosphate and fructose 6-phosphate. Outside the cell, however, the protein appears to function as a cytokine. A crystal structure of human PGI bound with 5-phosphoarabinonate, a strong inhibitor that mimics the cis-enediol(ate) intermediate of the reaction, has been determined at 2.5 A resolution. The structure helps to confirm the assignment of Glu357 as the base catalyst in the isomerase reaction.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1NUH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 and PA5 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NUH OCA].
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1NUH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=PA5:'>PA5</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NUH OCA].
==Reference==
==Reference==
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[[Category: neurotrophic growth factor]]
[[Category: neurotrophic growth factor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:25:46 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:10:06 2008''

Revision as of 12:10, 21 February 2008


1nuh, resolution 2.51Å

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The crystal structure of human phosphoglucose isomerase complexed with 5-phosphoarabinonate

Contents

Overview

Phosphoglucose isomerase (PGI) is a workhorse enzyme of carbohydrate metabolism that interconverts glucose 6-phosphate and fructose 6-phosphate. Outside the cell, however, the protein appears to function as a cytokine. A crystal structure of human PGI bound with 5-phosphoarabinonate, a strong inhibitor that mimics the cis-enediol(ate) intermediate of the reaction, has been determined at 2.5 A resolution. The structure helps to confirm the assignment of Glu357 as the base catalyst in the isomerase reaction.

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

1NUH is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Glucose-6-phosphate isomerase, with EC number 5.3.1.9 Full crystallographic information is available from OCA.

Reference

The structure of human phosphoglucose isomerase complexed with a transition-state analogue., Davies C, Muirhead H, Chirgwin J, Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):1111-3. Epub 2003, May 23. PMID:12777791

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