9gpb
From Proteopedia
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|PDB= 9gpb |SIZE=350|CAPTION= <scene name='initialview01'>9gpb</scene>, resolution 2.9Å | |PDB= 9gpb |SIZE=350|CAPTION= <scene name='initialview01'>9gpb</scene>, resolution 2.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |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> | ||
}} | }} | ||
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[[Category: Barford, D.]] | [[Category: Barford, D.]] | ||
[[Category: Johnson, L N.]] | [[Category: Johnson, L N.]] | ||
| - | [[Category: PLP]] | ||
| - | [[Category: SO4]] | ||
[[Category: glycogen phosphorylase]] | [[Category: glycogen phosphorylase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:46:07 2008'' |
Revision as of 02:46, 31 March 2008
| |||||||
| , resolution 2.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Phosphorylase, with EC number 2.4.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Mon Mar 31 05:46:07 2008
