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spinqualitylabelsall models 1umg, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 MG, 2FP and MPD 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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