1umg

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(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 ...)
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caption="1umg, resolution 1.80&Aring;" />
'''Crystal strucure of fructose-1,6-bisphosphatase'''<br />
'''Crystal strucure of fructose-1,6-bisphosphatase'''<br />
==Overview==
==Overview==
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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.
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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==
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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].
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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==
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[[Category: three metal-assisted mechanism]]
[[Category: three metal-assisted mechanism]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:12:56 2007''
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''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

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