1fj9: Difference between revisions

Revision as of 03:21, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1fj9.png

Template:STRUCTURE 1fj9

FRUCTOSE-1,6-BISPHOSPHATASE (MUTANT Y57W) PRODUCTS/ZN/AMP COMPLEX (T-STATE)FRUCTOSE-1,6-BISPHOSPHATASE (MUTANT Y57W) PRODUCTS/ZN/AMP COMPLEX (T-STATE)

Template:ABSTRACT PUBMED 10998248

About this StructureAbout this Structure

1FJ9 is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

ReferenceReference

Tryptophan fluorescence reveals the conformational state of a dynamic loop in recombinant porcine fructose-1,6-bisphosphatase., Nelson SW, Iancu CV, Choe JY, Honzatko RB, Fromm HJ, Biochemistry. 2000 Sep 12;39(36):11100-6. PMID:10998248

Page seeded by OCA on Tue Jul 1 03:21:17 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1fj9|  PDB=1fj9  |  SCENE=  }}
-'''FRUCTOSE-1,6-BISPHOSPHATASE (MUTANT Y57W) PRODUCTS/ZN/AMP COMPLEX (T-STATE)'''
+===FRUCTOSE-1,6-BISPHOSPHATASE (MUTANT Y57W) PRODUCTS/ZN/AMP COMPLEX (T-STATE)===
-==Overview==
+<!--
-Wild-type porcine fructose-1,6-bisphosphatase (FBPase) has no tryptophan residues. Hence, the mutation of Try57 to tryptophan places a unique fluorescent probe in the structural element (loop 52-72) putatively responsible for allosteric regulation of catalysis. On the basis of steady-state kinetics, circular dichroism spectroscopy, and X-ray crystallography, the mutation has little effect on the functional and structural properties of the enzyme. Fluorescence intensity from the Trp57 mutant is maximal in the presence of divalent cations, fructose 6-phosphate and orthophosphate, which together stabilize an R-state conformation in which loop 52-72 is engaged with the active site. The level of fluorescence emission decreases monotonically with increasing levels of AMP, an allosteric inhibitor, which promotes the T-state, disengaged-loop conformation. The titration of various metal-product complexes of the Trp57 mutant with fructose 2,6-bisphosphate (F26P(2)) causes similar decreases in fluorescence, suggesting that F26P(2) and AMP individually induce similar conformational states in FBPase. Fluorescence spectra, however, are sensitive to the type of divalent cation (Zn(2+), Mn(2+), or Mg(2+)) and suggest conformations in addition to the R-state, loop-engaged and T-state, loop-disengaged forms of FBPase. The work presented here demonstrates the utility of fluorescence spectroscopy in probing the conformational dynamics of FBPase.
+The line below this paragraph, {{ABSTRACT_PUBMED_10998248}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_10998248}}
 ==About this Structure==
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 [[Category: Bisphosphatase]]
 [[Category: Gluconeogenesis]]
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