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J. Biol. Chem., Vol. 277, Issue 25, 22863-22874, June 21, 2002
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From the 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.
The atomic coordinates and the structure factors (code 1LBV, 1LBW, 1LBX, 1LBY, 1LBZ) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).
Crystal Structure of a Dual Activity IMPase/FBPase
(AF2372) from Archaeoglobus fulgidus
THE STORY OF A MOBILE LOOP*
§,
,,,
Department of Chemistry, Merkert Chemistry
Center, Boston College, Chestnut Hill, Massachusetts 02467, the
** Department of Physiology and Biophysics, Boston University
School of Medicine, Boston, Massachusetts 02118, and the
¶ Department of Biochemistry and Cell Biology, W. M. Keck Center
for Computational Biology, Rice University, Houston, Texas 77005
*
This work was supported in part by Grant 2T15LM07093 from
the W. M. Keck Center for Computational Biology (to B. S.) and by Grant MCB-9978250 from the NSF, National Institutes of Health (to M. F. R.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Dept. of Biochemical Sciences, University of
Rome "La Sapienza," I-00185 Rome, Italy.
To whom correspondence should be addressed. Tel.: 713-348-3346;
Fax: 713-348-5154; Email: stec@bioc.rice.edu.
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