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1n8t
From Proteopedia
(New page: 200px<br /><applet load="1n8t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n8t, resolution 2.50Å" /> '''The crystal structur...) |
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| - | [[Image:1n8t.gif|left|200px]]<br /><applet load="1n8t" size=" | + | [[Image:1n8t.gif|left|200px]]<br /><applet load="1n8t" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1n8t, resolution 2.50Å" /> | caption="1n8t, resolution 2.50Å" /> | ||
'''The crystal structure of phosphoglucose isomerase from rabbit muscle'''<br /> | '''The crystal structure of phosphoglucose isomerase from rabbit muscle'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Phosphoglucose isomerase (PGI) is a housekeeping enzyme of metabolism that | + | Phosphoglucose isomerase (PGI) is a housekeeping enzyme of metabolism that catalyses the interconversion of glucose 6-phosphate and fructose 6-phosphate, with roles in the glycolytic and gluconeogenic pathways. PGI is also a multifunctional protein that manifests the properties of a cytokine in a wide array of cellular processes, including the production of immunoglobulin by B cells and tumour-cell differentiation. The crystal structure of PGI in the native form from rabbit muscle has been solved at a resolution of 2.5 A by a combination of multiple isomorphous replacement and multi-crystal averaging techniques. Comparison with published structures of rabbit PGI in complex with three inhibitors and with the substrate fructose 6-phosphate reveals a number of conformational changes that may be associated with catalytic function. These occur in the small domain around the sugar phosphate-binding site, in a small helix carrying His388 and in a helix near the C-terminal end. One of these may be the structural rearrangement that has been postulated to be the rate-limiting step for catalysis. |
==About this Structure== | ==About this Structure== | ||
| - | 1N8T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. 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:// | + | 1N8T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. 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=1N8T OCA]. |
==Reference== | ==Reference== | ||
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[[Category: glycolysis]] | [[Category: glycolysis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:03:30 2008'' |
Revision as of 12:03, 21 February 2008
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The crystal structure of phosphoglucose isomerase from rabbit muscle
Overview
Phosphoglucose isomerase (PGI) is a housekeeping enzyme of metabolism that catalyses the interconversion of glucose 6-phosphate and fructose 6-phosphate, with roles in the glycolytic and gluconeogenic pathways. PGI is also a multifunctional protein that manifests the properties of a cytokine in a wide array of cellular processes, including the production of immunoglobulin by B cells and tumour-cell differentiation. The crystal structure of PGI in the native form from rabbit muscle has been solved at a resolution of 2.5 A by a combination of multiple isomorphous replacement and multi-crystal averaging techniques. Comparison with published structures of rabbit PGI in complex with three inhibitors and with the substrate fructose 6-phosphate reveals a number of conformational changes that may be associated with catalytic function. These occur in the small domain around the sugar phosphate-binding site, in a small helix carrying His388 and in a helix near the C-terminal end. One of these may be the structural rearrangement that has been postulated to be the rate-limiting step for catalysis.
About this Structure
1N8T is a Single protein structure of sequence from Oryctolagus cuniculus. Active as Glucose-6-phosphate isomerase, with EC number 5.3.1.9 Full crystallographic information is available from OCA.
Reference
Structure of native phosphoglucose isomerase from rabbit: conformational changes associated with catalytic function., Davies C, Muirhead H, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):453-65. Epub 2003, Feb 21. PMID:12595702
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