2pgi: Difference between revisions

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[[Image:2pgi.gif|left|200px]]<br />

[[Image:2pgi.gif|left|200px]]<br /><applet load="2pgi" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="2pgi" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="2pgi, resolution 2.3Å" />

'''THE CRYSTAL STRUCTURE OF PHOSPHOGLUCOSE ISOMERASE-AN ENZYME WITH AUTOCRINE MOTILITY FACTOR ACTIVITY IN TUMOR CELLS'''<br />

==Overview==

Phosphoglucose isomerase (PGI) plays a central role in both the glycolysis, and the gluconeogenesis pathways. We present here the complete crystal, structure of PGI from Bacillus stearothermophilus at 2.3-A resolution. We, show that PGI has cell-motility-stimulating activity on mouse colon cancer, cells similar to that of endogenous autocrine motility factor (AMF). PGI, can also enhance neurite outgrowth on neuronal progenitor cells similar to, that observed for neuroleukin. The results confirm that PGI is neuroleukin, and AMF. PGI has an open twisted alpha/beta structural motif consisting of, two globular domains and two protruding parts. Based on this, substrate-free structure, together with the previously published, biological, biochemical, and modeling results, we postulate a possible, substrate-binding site that is located within the domains' interface for, PGI and AMF. In addition, the structure provides evidence suggesting that, the top part of the large domain together with one of the protruding loops, might participate in inducing the neurotrophic activity.

Phosphoglucose isomerase (PGI) plays a central role in both the glycolysis and the gluconeogenesis pathways. We present here the complete crystal structure of PGI from Bacillus stearothermophilus at 2.3-A resolution. We show that PGI has cell-motility-stimulating activity on mouse colon cancer cells similar to that of endogenous autocrine motility factor (AMF). PGI can also enhance neurite outgrowth on neuronal progenitor cells similar to that observed for neuroleukin. The results confirm that PGI is neuroleukin and AMF. PGI has an open twisted alpha/beta structural motif consisting of two globular domains and two protruding parts. Based on this substrate-free structure, together with the previously published biological, biochemical, and modeling results, we postulate a possible substrate-binding site that is located within the domains' interface for PGI and AMF. In addition, the structure provides evidence suggesting that the top part of the large domain together with one of the protruding loops might participate in inducing the neurotrophic activity.

==About this Structure==

2PGI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. The following page contains interesting information on the relation of 2PGI with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb89_1.html Aconitase and Iron Regulatory Protein 1]]. 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=2PGI OCA].

2PGI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. The following page contains interesting information on the relation of 2PGI with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb89_1.html Aconitase and Iron Regulatory Protein 1]]. 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=2PGI OCA].

==Reference==

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[[Category: Glucose-6-phosphate isomerase]]

[[Category: Single protein]]

[[Category: Chen, W.S.]]

[[Category: Chen, W S.]]

[[Category: Chou, C.C.]]

[[Category: Chou, C C.]]

[[Category: Hsiao, C.D.]]

[[Category: Hsiao, C D.]]

[[Category: Meng, M.]]

[[Category: Sun, Y.J.]]

[[Category: Sun, Y J.]]

[[Category: autocrinefactor]]

[[Category: crystallography]]

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[[Category: phosphoglucose isomerase]]

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@@ Line 1: / Line 1: @@
-[[Image:2pgi.gif|left|200px]]<br />
+[[Image:2pgi.gif|left|200px]]<br /><applet load="2pgi" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2pgi" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2pgi, resolution 2.3&Aring;" />
 '''THE CRYSTAL STRUCTURE OF PHOSPHOGLUCOSE ISOMERASE-AN ENZYME WITH AUTOCRINE MOTILITY FACTOR ACTIVITY IN TUMOR CELLS'''<br />
 ==Overview==
-Phosphoglucose isomerase (PGI) plays a central role in both the glycolysis, and the gluconeogenesis pathways. We present here the complete crystal, structure of PGI from Bacillus stearothermophilus at 2.3-A resolution. We, show that PGI has cell-motility-stimulating activity on mouse colon cancer, cells similar to that of endogenous autocrine motility factor (AMF). PGI, can also enhance neurite outgrowth on neuronal progenitor cells similar to, that observed for neuroleukin. The results confirm that PGI is neuroleukin, and AMF. PGI has an open twisted alpha/beta structural motif consisting of, two globular domains and two protruding parts. Based on this, substrate-free structure, together with the previously published, biological, biochemical, and modeling results, we postulate a possible, substrate-binding site that is located within the domains' interface for, PGI and AMF. In addition, the structure provides evidence suggesting that, the top part of the large domain together with one of the protruding loops, might participate in inducing the neurotrophic activity.
+Phosphoglucose isomerase (PGI) plays a central role in both the glycolysis and the gluconeogenesis pathways. We present here the complete crystal structure of PGI from Bacillus stearothermophilus at 2.3-A resolution. We show that PGI has cell-motility-stimulating activity on mouse colon cancer cells similar to that of endogenous autocrine motility factor (AMF). PGI can also enhance neurite outgrowth on neuronal progenitor cells similar to that observed for neuroleukin. The results confirm that PGI is neuroleukin and AMF. PGI has an open twisted alpha/beta structural motif consisting of two globular domains and two protruding parts. Based on this substrate-free structure, together with the previously published biological, biochemical, and modeling results, we postulate a possible substrate-binding site that is located within the domains' interface for PGI and AMF. In addition, the structure provides evidence suggesting that the top part of the large domain together with one of the protruding loops might participate in inducing the neurotrophic activity.
 ==About this Structure==
-PGI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. The following page contains interesting information on the relation of 2PGI with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb89_1.html Aconitase and Iron Regulatory Protein 1]]. 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=2PGI OCA].
+PGI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. The following page contains interesting information on the relation of 2PGI with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb89_1.html Aconitase and Iron Regulatory Protein 1]]. 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=2PGI OCA].
 ==Reference==
@@ Line 16: / Line 15: @@
 [[Category: Glucose-6-phosphate isomerase]]
 [[Category: Single protein]]
-[[Category: Chen, W.S.]]
+[[Category: Chen, W S.]]
-[[Category: Chou, C.C.]]
+[[Category: Chou, C C.]]
-[[Category: Hsiao, C.D.]]
+[[Category: Hsiao, C D.]]
 [[Category: Meng, M.]]
-[[Category: Sun, Y.J.]]
+[[Category: Sun, Y J.]]
 [[Category: autocrinefactor]]
 [[Category: crystallography]]
@@ Line 28: / Line 27: @@
 [[Category: phosphoglucose isomerase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:09:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:29:13 2008''