1yyz: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1yyz.gif|left|200px]]
{{Seed}}
[[Image:1yyz.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1yyz|  PDB=1yyz  |  SCENE=  }}  
{{STRUCTURE_1yyz|  PDB=1yyz  |  SCENE=  }}  


'''R-State AMP Complex Reveals Initial Steps of the Quaternary Transition of Fructose-1,6-bisphosphatase'''
===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.
The line below this paragraph, {{ABSTRACT_PUBMED_15767255}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15767255 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15767255}}


==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Glycolysis]]
[[Category: Glycolysis]]
[[Category: Intermediate state]]
[[Category: Intermediate state]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:58:52 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:27:56 2008''

Revision as of 04:28, 28 July 2008

File:1yyz.png

Template:STRUCTURE 1yyz

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

Template:ABSTRACT PUBMED 15767255

About this Structure

1YYZ 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

Page seeded by OCA on Mon Jul 28 07:27:56 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1yyz&oldid=687702"