1umg
From Proteopedia
| |||||||
| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | ST0318 (Sulfolobus tokodaii) | ||||||
| Activity: | Fructose-bisphosphatase, with EC number 3.1.3.11 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mon Mar 31 00:12:16 2008
Categories: Fructose-bisphosphatase | Single protein | Sulfolobus tokodaii | Fushinobu, S. | Nishimasu, H. | Shoun, H. | Wakagi, T. | Alpha-beta-beta-alpha four layer sandwich | Fructose-1,6-bisphosphatase | Hyperthermophilic archaea | Magnesium ion | Octamer | Phosphatase | Three metal-assisted mechanism
