Structural highlights
Function
[SUHB_ARCFU] Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, inositol-2-phosphate, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate and fructose-6-phosphate. May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Several hyperthermophilic organisms contain an unusual phosphatase that has dual activity toward inositol monophosphates and fructose 1,6-bisphosphate. The structure of the second member of this family, an FBPase/IMPase from Archaeoglobus fulgidus (AF2372), has been solved. This enzyme shares many kinetic and structural similarities with that of a previously solved enzyme from Methanococcus jannaschii (MJ0109). It also shows some kinetic differences in divalent metal ion binding as well as structural variations at the dimer interface that correlate with decreased thermal stability. The availability of different crystal forms allowed us to investigate the effect of the presence of ligands on the conformation of a mobile catalytic loop independently of the crystal packing. This conformational variability in AF2372 is compared with that observed in other members of this structural family that are sensitive or insensitive to submillimolar concentrations of Li(+). This analysis provides support for the previously proposed mechanism of catalysis involving three metal ions. A direct correlation of the loop conformation with strength of Li(+) inhibition provides a useful system of classification for this extended family of enzymes.
Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop.,Stieglitz KA, Johnson KA, Yang H, Roberts MF, Seaton BA, Head JF, Stec B J Biol Chem. 2002 Jun 21;277(25):22863-74. Epub 2002 Apr 8. PMID:11940584[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen L, Roberts MF. Overexpression, purification, and analysis of complementation behavior of E. coli SuhB protein: comparison with bacterial and archaeal inositol monophosphatases. Biochemistry. 2000 Apr 11;39(14):4145-53. PMID:10747806
- ↑ Stec B, Yang H, Johnson KA, Chen L, Roberts MF. MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase. Nat Struct Biol. 2000 Nov;7(11):1046-50. PMID:11062561 doi:10.1038/80968
- ↑ Stieglitz KA, Johnson KA, Yang H, Roberts MF, Seaton BA, Head JF, Stec B. Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop. J Biol Chem. 2002 Jun 21;277(25):22863-74. Epub 2002 Apr 8. PMID:11940584 doi:http://dx.doi.org/10.1074/jbc.M201042200
- ↑ Stieglitz KA, Johnson KA, Yang H, Roberts MF, Seaton BA, Head JF, Stec B. Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop. J Biol Chem. 2002 Jun 21;277(25):22863-74. Epub 2002 Apr 8. PMID:11940584 doi:http://dx.doi.org/10.1074/jbc.M201042200
