8gpb
From Proteopedia
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STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP
Overview
The crystal structures of activated R state glycogen phosphorylase a (GPa), and R and T state glycogen phosphorylase b (GPb) complexed with AMP have, been solved at 2.9 A, 2.9 A and 2.2 A resolution, respectively. The, structure of R state GPa is nearly identical to the structure of, sulphate-activated R state GPb, except in the region of Ser14, where there, is a covalently attached phosphate group in GPa and a non-covalently, attached sulphate group in GPb. The contacts made by the N-terminal tail, residues in R state GPa at the subunit interface of the functionally, active dimer are similar to those observed previously for T state GPa. The, quaternary and tertiary structural changes on the T to R transition allow, these interactions to be relayed to the catalytic site in R state GPa. ... [(full description)]
About this Structure
8GPB is a [Single protein] structure of sequence from [Oryctolagus cuniculus] with PLP and AMP as [ligands]. The following page contains interesting information on the relation of 8GPB with [Glycogen Phosphorylase].
Reference
Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP., Barford D, Hu SH, Johnson LN, J Mol Biol. 1991 Mar 5;218(1):233-60. PMID:1900534
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