9gpb
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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
OverviewOverview
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 StructureAbout this Structure
9GPB is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
ReferenceReference
The allosteric transition of glycogen phosphorylase., Barford D, Johnson LN, Nature. 1989 Aug 24;340(6235):609-16. PMID:2770867
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