1fpi
From Proteopedia
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Revision as of 13:07, 30 October 2007
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FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) COMPLEXED WITH AMP, 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND POTASSIUM IONS (100 MM)
Overview
Fructose-1,6-bisphosphatase (Fru-1,6-Pase; D-fructose-1,6-bisphosphate, 1-phosphohydrolase, EC 3.1.3.11) requires two divalent metal ions to, hydrolyze alpha-D-fructose 1,6-bisphosphate. Although not required for, catalysis, monovalent cations modify the enzyme activity; K+ and Tl+ ions, are activators, whereas Li+ ions are inhibitors. Their mechanisms of, action are still unknown. We report here crystallographic structures of, pig kidney Fru-1,6-Pase complexed with K+, Tl+, or both Tl+ and Li+. In, the T form Fru-1,6-Pase complexed with the substrate analogue, 2,5-anhydro-D-glucitol 1,6-bisphosphate (AhG-1,6-P2) and Tl+ or K+ ions, three Tl+ or K+ binding sites are found. Site 1 is defined by Glu-97, Asp-118, Asp-121, Glu-280, and a 1-phosphate oxygen of AhG-1,6-P2; site 2, is defined by ... [(full description)]
About this Structure
1FPI is a [Single protein] structure of sequence from [Sus scrofa] with K, AMP and AHG as [ligands]. Active as [Fructose-bisphosphatase], with EC number [3.1.3.11]. Structure known Active Sites: AC1, AC2, AM1, AM2, PO1, PO2, PO3, PO4, PO5 and PO6. Full crystallographic information is available from [OCA].
Reference
Crystallographic evidence for the action of potassium, thallium, and lithium ions on fructose-1,6-bisphosphatase., Villeret V, Huang S, Fromm HJ, Lipscomb WN, Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8916-20. PMID:7568043
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