We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1fj6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fj6.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1fj6.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fj6| PDB=1fj6 | SCENE= }}
{{STRUCTURE_1fj6| PDB=1fj6 | SCENE= }}
-
'''FRUCTOSE-1,6-BISPHOSPHATASE (MUTANT Y57W) PRODUCT/ZN COMPLEX (R-STATE)'''
+
===FRUCTOSE-1,6-BISPHOSPHATASE (MUTANT Y57W) PRODUCT/ZN COMPLEX (R-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
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10998248 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10998248}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Bisphosphatase]]
[[Category: Bisphosphatase]]
[[Category: Gluconeogenesis]]
[[Category: Gluconeogenesis]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:23:25 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:21:07 2008''

Revision as of 00:21, 1 July 2008

Image:1fj6.png

Template:STRUCTURE 1fj6

FRUCTOSE-1,6-BISPHOSPHATASE (MUTANT Y57W) PRODUCT/ZN COMPLEX (R-STATE)

Template:ABSTRACT PUBMED 10998248

About this Structure

1FJ6 is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

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 03:21:07 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fj6"
Personal tools