1n8t: Difference between revisions

Line 1:

[[Image:1n8t.gif|left|200px]]<br /><applet load="1n8t" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1n8t.gif|left|200px]]<br /><applet load="1n8t" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1n8t, resolution 2.50Å" />

'''The crystal structure of phosphoglucose isomerase from rabbit muscle'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1N8T OCA].

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==

Line 20:

[[Category: glycolysis]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 22~~:03:~~38 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:03:30 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1n8t.gif|left|200px]]<br /><applet load="1n8t" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1n8t.gif|left|200px]]<br /><applet load="1n8t" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1n8t, resolution 2.50&Aring;" />
 '''The crystal structure of phosphoglucose isomerase from rabbit muscle'''<br />
 ==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.
+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==
-N8T 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N8T OCA].
+N8T 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==
@@ Line 20: / Line 20: @@
 [[Category: glycolysis]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:03:38 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:03:30 2008''