9gpb
From Proteopedia
(New page: 200px<br /><applet load="9gpb" size="450" color="white" frame="true" align="right" spinBox="true" caption="9gpb, resolution 2.9Å" /> '''THE ALLOSTERIC TRANSI...) |
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| - | [[Image:9gpb.gif|left|200px]]<br /><applet load="9gpb" size=" | + | [[Image:9gpb.gif|left|200px]]<br /><applet load="9gpb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="9gpb, resolution 2.9Å" /> | caption="9gpb, resolution 2.9Å" /> | ||
'''THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE'''<br /> | '''THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of R-state glycogen phosphorylase b has been | + | 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== | ==About this Structure== | ||
| - | 9GPB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with SO4 and PLP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 9GPB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9GPB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Barford, D.]] | [[Category: Barford, D.]] | ||
| - | [[Category: Johnson, L | + | [[Category: Johnson, L N.]] |
[[Category: PLP]] | [[Category: PLP]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: glycogen phosphorylase]] | [[Category: glycogen phosphorylase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:18:30 2008'' |
Revision as of 17:18, 21 February 2008
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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 with and as ligands. Active as Phosphorylase, with EC number 2.4.1.1 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
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