This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1umg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1umg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1umg, resolution 1.80&Aring;" /> '''Crystal strucure of ...)
Line 1: Line 1:
-
[[Image:1umg.gif|left|200px]]<br /><applet load="1umg" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1umg.gif|left|200px]]<br /><applet load="1umg" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1umg, resolution 1.80&Aring;" />
caption="1umg, resolution 1.80&Aring;" />
'''Crystal strucure of fructose-1,6-bisphosphatase'''<br />
'''Crystal strucure of fructose-1,6-bisphosphatase'''<br />
==Overview==
==Overview==
-
As the first structure of the novel class of fructose-1,6-bisphosphatase, (FBPase) present in thermophilic archaea, we solved the crystal structure, of the ST0318 gene product (St-Fbp) of Sulfolobus tokodaii strain 7. The, St-Fbp structure comprises a homooctamer of the 422 point-group. The, protein folds as a four-layer alpha-beta-beta-alpha sandwich with a novel, topology, which is completely different from the sugar phosphatase fold., The structure contains an unhydrolyzed FBP molecule in the open-keto form, as well as four hexacoordinated magnesium ions around the 1-phosphoryl, group of FBP. The arrangement of the catalytic side chains and metal, ligands is consistent with the three-metal ion assisted catalysis proposed, for conventional FBPases. The structure provides an insight into the, structural basis of the strict substrate specificity of St-Fbp.
+
As the first structure of the novel class of fructose-1,6-bisphosphatase (FBPase) present in thermophilic archaea, we solved the crystal structure of the ST0318 gene product (St-Fbp) of Sulfolobus tokodaii strain 7. The St-Fbp structure comprises a homooctamer of the 422 point-group. The protein folds as a four-layer alpha-beta-beta-alpha sandwich with a novel topology, which is completely different from the sugar phosphatase fold. The structure contains an unhydrolyzed FBP molecule in the open-keto form, as well as four hexacoordinated magnesium ions around the 1-phosphoryl group of FBP. The arrangement of the catalytic side chains and metal ligands is consistent with the three-metal ion assisted catalysis proposed for conventional FBPases. The structure provides an insight into the structural basis of the strict substrate specificity of St-Fbp.
==About this Structure==
==About this Structure==
-
1UMG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_tokodaii Sulfolobus tokodaii] with MG, 2FP and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UMG OCA].
+
1UMG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_tokodaii Sulfolobus tokodaii] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=2FP:'>2FP</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMG OCA].
==Reference==
==Reference==
Line 30: Line 30:
[[Category: three metal-assisted mechanism]]
[[Category: three metal-assisted mechanism]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:12:56 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:26:07 2008''

Revision as of 13:26, 21 February 2008

Image:1umg.gif

1umg, resolution 1.80Å

Drag the structure with the mouse to rotate

Crystal strucure of fructose-1,6-bisphosphatase

Overview

As the first structure of the novel class of fructose-1,6-bisphosphatase (FBPase) present in thermophilic archaea, we solved the crystal structure of the ST0318 gene product (St-Fbp) of Sulfolobus tokodaii strain 7. The St-Fbp structure comprises a homooctamer of the 422 point-group. The protein folds as a four-layer alpha-beta-beta-alpha sandwich with a novel topology, which is completely different from the sugar phosphatase fold. The structure contains an unhydrolyzed FBP molecule in the open-keto form, as well as four hexacoordinated magnesium ions around the 1-phosphoryl group of FBP. The arrangement of the catalytic side chains and metal ligands is consistent with the three-metal ion assisted catalysis proposed for conventional FBPases. The structure provides an insight into the structural basis of the strict substrate specificity of St-Fbp.

About this Structure

1UMG is a Single protein structure of sequence from Sulfolobus tokodaii with , and as ligands. Active as Fructose-bisphosphatase, with EC number 3.1.3.11 Full crystallographic information is available from OCA.

Reference

The first crystal structure of the novel class of fructose-1,6-bisphosphatase present in thermophilic archaea., Nishimasu H, Fushinobu S, Shoun H, Wakagi T, Structure. 2004 Jun;12(6):949-59. PMID:15274916

Page seeded by OCA on Thu Feb 21 15:26:07 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1umg"
Personal tools