9gpb
From Proteopedia
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 Sun May 4 22:52:59 2008
