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[[Image:9gpb.gif|left|200px]]
[[Image:9gpb.gif|left|200px]]


{{Structure
<!--
|PDB= 9gpb |SIZE=350|CAPTION= <scene name='initialview01'>9gpb</scene>, resolution 2.9&Aring;
The line below this paragraph, containing "STRUCTURE_9gpb", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </span>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_9gpb| PDB=9gpb  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=9gpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9gpb OCA], [http://www.ebi.ac.uk/pdbsum/9gpb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=9gpb RCSB]</span>
}}


'''THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE'''
'''THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE'''
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[[Category: Barford, D.]]
[[Category: Barford, D.]]
[[Category: Johnson, L N.]]
[[Category: Johnson, L N.]]
[[Category: glycogen phosphorylase]]
[[Category: Glycogen phosphorylase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:52:59 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:46:07 2008''

Revision as of 19:53, 4 May 2008

File:9gpb.gif

Template:STRUCTURE 9gpb

THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE


Overview

The crystal structure of R-state glycogen phosphorylase b has been determined at 2.9 A resolution. A comparison of T-state and R-state structures of the enzyme explains its cooperative behaviour on ligand binding and the allosteric regulation of its activity. Communication between catalytic sites of the dimer is provided by a change in packing geometry of two helices linking each site with the subunit interface. Activation by AMP or by phosphorylation results in a quaternary conformational change that switches these two helices into the R-state conformation.

About this Structure

9GPB is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

The allosteric transition of glycogen phosphorylase., Barford D, Johnson LN, Nature. 1989 Aug 24;340(6235):609-16. PMID:2770867 Page seeded by OCA on Sun May 4 22:52:59 2008

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