1q9d: Difference between revisions

Revision as of 18:10, 27 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:1q9d.png

Template:STRUCTURE 1q9d

Fructose-1,6-bisphosphatase Complexed with a New Allosteric Site Inhibitor (I-State)Fructose-1,6-bisphosphatase Complexed with a New Allosteric Site Inhibitor (I-State)

Template:ABSTRACT PUBMED 14530289

About this StructureAbout this Structure

1Q9D is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

ReferenceReference

Inhibition of fructose-1,6-bisphosphatase by a new class of allosteric effectors., Choe JY, Nelson SW, Arienti KL, Axe FU, Collins TL, Jones TK, Kimmich RD, Newman MJ, Norvell K, Ripka WC, Romano SJ, Short KM, Slee DH, Fromm HJ, Honzatko RB, J Biol Chem. 2003 Dec 19;278(51):51176-83. Epub 2003 Oct 6. PMID:14530289

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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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-[[Image:1q9d.gif|left|200px]]
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 {{STRUCTURE_1q9d|  PDB=1q9d  |  SCENE=  }}
-'''Fructose-1,6-bisphosphatase Complexed with a New Allosteric Site Inhibitor (I-State)'''
+===Fructose-1,6-bisphosphatase Complexed with a New Allosteric Site Inhibitor (I-State)===
-==Overview==
+<!--
-A highly constrained pseudo-tetrapeptide (OC252-324) further defines a new allosteric binding site located near the center of fructose-1,6-bisphosphatase. In a crystal structure, pairs of inhibitory molecules bind to opposite faces of the enzyme tetramer. Each ligand molecule is in contact with three of four subunits of the tetramer, hydrogen bonding with the side chain of Asp187 and the backbone carbonyl of residue 71, and electrostatically interacting with the backbone carbonyl of residue 51. The ligated complex adopts a quaternary structure between the canonical R- and T-states of fructose-1,6-bisphosphatase, and yet a dynamic loop essential for catalysis (residues 52-72) is in a conformation identical to that of the T-state enzyme. Inhibition by the pseudo-tetrapeptide is cooperative (Hill coefficient of 2), synergistic with both AMP and fructose 2,6-bisphosphate, noncompetitive with respect to Mg2+, and uncompetitive with respect to fructose 1,6-bisphosphate. The ligand dramatically lowers the concentration at which substrate inhibition dominates the kinetics of fructose-1,6-bisphosphatase. Elevated substrate concentrations employed in kinetic screens may have facilitated the discovery of this uncompetitive inhibitor. Moreover, the inhibitor could mimic an unknown natural effector of fructose-1,6-bisphosphatase, as it interacts strongly with a conserved residue of undetermined functional significance.
+The line below this paragraph, {{ABSTRACT_PUBMED_14530289}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14530289 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14530289}}
 ==About this Structure==
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 [[Category: Bisphosphatase]]
 [[Category: Hydrolase]]
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