9gpb: Difference between revisions
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[[Image:9gpb.gif|left|200px]] | [[Image:9gpb.gif|left|200px]] | ||
'''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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| 9gpb, resolution 2.9Å | |||||||||||||
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| Ligands: | SO4 and PLP | ||||||||||||
| 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
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