1LBW
Crystal Structure of apo-form (P32) of dual activity FBPase/IMPase (AF2372) from Archaeoglobus fulgidus
Summary for 1LBW
| Entry DOI | 10.2210/pdb1lbw/pdb |
| Related | 1LBV 1LBX 1LBY 1LBZ |
| Descriptor | fructose 1,6-bisphosphatase/inositol monophosphatase (2 entities in total) |
| Functional Keywords | dual activity, fbpase, impase, archaeal phosphatase, apo-form, hydrolase |
| Biological source | Archaeoglobus fulgidus |
| Total number of polymer chains | 2 |
| Total formula weight | 56005.68 |
| Authors | Stieglitz, K.A.,Johnson, K.A.,Yang, H.,Roberts, M.F.,Seaton, B.A.,Head, J.F.,Stec, B. (deposition date: 2002-04-04, release date: 2002-05-22, Last modification date: 2023-08-16) |
| Primary citation | Stieglitz, K.A.,Johnson, K.A.,Yang, H.,Roberts, M.F.,Seaton, B.A.,Head, J.F.,Stec, B. Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop. J.Biol.Chem., 277:22863-22874, 2002 Cited by PubMed Abstract: 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. PubMed: 11940584DOI: 10.1074/jbc.M201042200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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