1yz0

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[[Image:1yz0.gif|left|200px]]<br /><applet load="1yz0" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1yz0.gif|left|200px]]
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caption="1yz0, resolution 2.07&Aring;" />
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'''R-State AMP Complex Reveals Initial Steps of the Quaternary Transition of Fructose-1,6-bisphosphatase'''<br />
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{{Structure
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|PDB= 1yz0 |SIZE=350|CAPTION= <scene name='initialview01'>1yz0</scene>, resolution 2.07&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=AMP:ADENOSINE MONOPHOSPHATE'>AMP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11]
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|GENE= FBP1, FBP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 Sus scrofa])
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}}
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'''R-State AMP Complex Reveals Initial Steps of the Quaternary Transition of Fructose-1,6-bisphosphatase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1YZ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=F6P:'>F6P</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=AMP:'>AMP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YZ0 OCA].
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1YZ0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YZ0 OCA].
==Reference==
==Reference==
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R-state AMP complex reveals initial steps of the quaternary transition of fructose-1,6-bisphosphatase., Iancu CV, Mukund S, Fromm HJ, Honzatko RB, J Biol Chem. 2005 May 20;280(20):19737-45. Epub 2005 Mar 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15767255 15767255]
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R-state AMP complex reveals initial steps of the quaternary transition of fructose-1,6-bisphosphatase., Iancu CV, Mukund S, Fromm HJ, Honzatko RB, J Biol Chem. 2005 May 20;280(20):19737-45. Epub 2005 Mar 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15767255 15767255]
[[Category: Fructose-bisphosphatase]]
[[Category: Fructose-bisphosphatase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: allosteric enzymes; intermediate states; glycolysis; gluconeogenesis]]
[[Category: allosteric enzymes; intermediate states; glycolysis; gluconeogenesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:10:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:29:15 2008''

Revision as of 13:29, 20 March 2008


PDB ID 1yz0

Drag the structure with the mouse to rotate
, resolution 2.07Å
Ligands: , and
Gene: FBP1, FBP (Sus scrofa)
Activity: Fructose-bisphosphatase, with EC number 3.1.3.11
Coordinates: save as pdb, mmCIF, xml



R-State AMP Complex Reveals Initial Steps of the Quaternary Transition of Fructose-1,6-bisphosphatase


Overview

AMP transforms fructose-1,6-bisphosphatase from its active R-state to its inactive T-state; however, the mechanism of that transformation is poorly understood. The mutation of Ala(54) to leucine destabilizes the T-state of fructose-1,6-bisphosphatase. The mutant enzyme retains wild-type levels of activity, but the concentration of AMP that causes 50% inhibition increases 50-fold. In the absence of AMP, the Leu(54) enzyme adopts an R-state conformation nearly identical to that of the wild-type enzyme. The mutant enzyme, however, grows in two crystal forms in the presence of saturating AMP. In one form, the AMP-bound tetramer is in a T-like conformation, whereas in the other form, the AMP-bound tetramer is in a R-like conformation. The latter reveals conformational changes in two helices due to the binding of AMP. Helix H1 moves toward the center of the tetramer and displaces Ile(10) from a hydrophobic pocket. The displacement of Ile(10) exposes a hydrophobic surface critical to interactions that stabilize the T-state. Helix H2 moves away from the center of the tetramer, breaking hydrogen bonds with a buried loop (residues 187-195) in an adjacent subunit. The same hydrogen bonds reform but only after the quaternary transition to the T-state. Proposed here is a model that accounts for the quaternary transition and cooperativity in the inhibition of catalysis by AMP.

About this Structure

1YZ0 is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

R-state AMP complex reveals initial steps of the quaternary transition of fructose-1,6-bisphosphatase., Iancu CV, Mukund S, Fromm HJ, Honzatko RB, J Biol Chem. 2005 May 20;280(20):19737-45. Epub 2005 Mar 14. PMID:15767255

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