1umg
From Proteopedia
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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
Categories: Fructose-bisphosphatase | Single protein | Sulfolobus tokodaii | Fushinobu, S. | Nishimasu, H. | Shoun, H. | Wakagi, T. | 2FP | MG | MPD | 6-bisphosphatase | Alpha-beta-beta-alpha four layer sandwich | Fructose-1 | Hyperthermophilic archaea | Magnesium ion | Octamer | Phosphatase | Three metal-assisted mechanism
