1UMG

Crystal structure of fructose-1,6-bisphosphatase

Summary for 1UMG

• Entry DOI: 10.2210/pdb1umg/pdb
• Descriptor: 385aa long conserved hypothetical protein, MAGNESIUM ION, 1,6-FRUCTOSE DIPHOSPHATE (LINEAR FORM), ... (5 entities in total)
• Functional Keywords: fructose-1, 6-bisphosphatase, hyperthermophilic archaea, alpha-beta-beta-alpha four layer sandwich, magnesium ion, phosphatase, octamer, three metal-assisted mechanism, hydrolase
• Biological source: Sulfolobus tokodaii str. 7
• Total number of polymer chains: 1
• Total formula weight: 40653.57

Authors

Nishimasu, H.,Fushinobu, S.,Shoun, H.,Wakagi, T. (deposition date: 2003-09-30, release date: 2004-07-13, Last modification date: 2023-12-27)

Primary citation

Nishimasu, H.,Fushinobu, S.,Shoun, H.,Wakagi, T.
The first crystal structure of the novel class of fructose-1,6-bisphosphatase present in thermophilic archaea.
Structure, 12:949-959, 2004

PubMed Abstract: 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.

PubMed: 15274916
DOI: 10.1016/j.str.2004.03.026

Experimental method

X-RAY DIFFRACTION (1.8 Å)