1lbx: Difference between revisions
New page: left|200px<br /><applet load="1lbx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lbx, resolution 2.4Å" /> '''Crystal Structure of ... |
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[[Image:1lbx.gif|left|200px]]<br /><applet load="1lbx" size=" | [[Image:1lbx.gif|left|200px]]<br /><applet load="1lbx" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1lbx, resolution 2.4Å" /> | caption="1lbx, resolution 2.4Å" /> | ||
'''Crystal Structure of a ternary complex of dual activity FBPase/IMPase (AF2372) from Archaeoglobus fulgidus with Calcium ions and D-myo-Inositol-1-Phosphate'''<br /> | '''Crystal Structure of a ternary complex of dual activity FBPase/IMPase (AF2372) from Archaeoglobus fulgidus with Calcium ions and D-myo-Inositol-1-Phosphate'''<br /> | ||
==Overview== | ==Overview== | ||
Several hyperthermophilic organisms contain an unusual phosphatase that | 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. | ||
==About this Structure== | ==About this Structure== | ||
1LBX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with CA and IPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1LBX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=IPD:'>IPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LBX OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Archaeoglobus fulgidus]] | [[Category: Archaeoglobus fulgidus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Head, J | [[Category: Head, J F.]] | ||
[[Category: Johnson, K | [[Category: Johnson, K A.]] | ||
[[Category: Roberts, M | [[Category: Roberts, M F.]] | ||
[[Category: Seaton, B | [[Category: Seaton, B A.]] | ||
[[Category: Stec, B.]] | [[Category: Stec, B.]] | ||
[[Category: Stieglitz, K | [[Category: Stieglitz, K A.]] | ||
[[Category: Yang, H.]] | [[Category: Yang, H.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: ternary complex with metal and substrate]] | [[Category: ternary complex with metal and substrate]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:43:30 2008'' | ||
Revision as of 14:43, 21 February 2008
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Crystal Structure of a ternary complex of dual activity FBPase/IMPase (AF2372) from Archaeoglobus fulgidus with Calcium ions and D-myo-Inositol-1-Phosphate
OverviewOverview
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.
About this StructureAbout this Structure
1LBX is a Single protein structure of sequence from Archaeoglobus fulgidus with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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
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