9gpb
From Proteopedia
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| - | [[Image:9gpb.gif|left|200px]] | + | [[Image:9gpb.gif|left|200px]] |
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| - | '''THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE''' | + | {{Structure |
| + | |PDB= 9gpb |SIZE=350|CAPTION= <scene name='initialview01'>9gpb</scene>, resolution 2.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 9GPB is a [ | + | 9GPB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9GPB OCA]. |
==Reference== | ==Reference== | ||
| - | The allosteric transition of glycogen phosphorylase., Barford D, Johnson LN, Nature. 1989 Aug 24;340(6235):609-16. PMID:[http:// | + | The allosteric transition of glycogen phosphorylase., Barford D, Johnson LN, Nature. 1989 Aug 24;340(6235):609-16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2770867 2770867] |
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Phosphorylase]] | [[Category: Phosphorylase]] | ||
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[[Category: glycogen phosphorylase]] | [[Category: glycogen phosphorylase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:16:20 2008'' |
Revision as of 17:16, 20 March 2008
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| , resolution 2.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Phosphorylase, with EC number 2.4.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 19:16:20 2008
