1lbv: Difference between revisions

Revision as of 12:17, 2 July 2008

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File:1lbv.png

Template:STRUCTURE 1lbv

Crystal Structure of apo-form (P21) of dual activity FBPase/IMPase (AF2372) from Archaeoglobus fulgidusCrystal Structure of apo-form (P21) of dual activity FBPase/IMPase (AF2372) from Archaeoglobus fulgidus

Template:ABSTRACT PUBMED 11940584

About this StructureAbout this Structure

1LBV is a Single protein structure of sequence from Archaeoglobus fulgidus. 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of apo-form (P21) of dual activity FBPase/IMPase (AF2372) from Archaeoglobus fulgidus'''
+===Crystal Structure of apo-form (P21) of dual activity FBPase/IMPase (AF2372) from Archaeoglobus fulgidus===
-==Overview==
+<!--
-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 line below this paragraph, {{ABSTRACT_PUBMED_11940584}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_11940584}}
 ==About this Structure==
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 [[Category: Fbpase]]
 [[Category: Impase]]
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