9gpb

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[[Image:9gpb.gif|left|200px]]
[[Image:9gpb.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 9gpb |SIZE=350|CAPTION= <scene name='initialview01'>9gpb</scene>, resolution 2.9&Aring;
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The line below this paragraph, containing "STRUCTURE_9gpb", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_9gpb| PDB=9gpb | SCENE= }}
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|RELATEDENTRY=
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|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>
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}}
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'''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.]]
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[[Category: glycogen phosphorylase]]
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[[Category: Glycogen phosphorylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:52:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:46:07 2008''
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Revision as of 19:53, 4 May 2008

Image: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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