|
type |
Journal Article |
authors |
Barford, D.; Johnson, L. N. |
title |
The allosteric transition of glycogen phosphorylase |
journal |
Nature |
Activity |
2.4.1.1 |
ui |
89365154 |
year |
(1989) |
volume |
340 |
number |
6235 |
pages |
609-16. |
| |
keywords |
*Allosteric Regulation |
abstract |
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. |
last changed |
2002/11/12 16:17 |
|