9GPB
THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE
Summary for 9GPB
| Entry DOI | 10.2210/pdb9gpb/pdb |
| Descriptor | Glycogen phosphorylase, muscle form, SULFATE ION (2 entities in total) |
| Functional Keywords | glycogen phosphorylase |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Total number of polymer chains | 4 |
| Total formula weight | 391230.04 |
| Authors | Barford, D.,Johnson, L.N. (deposition date: 1990-12-17, release date: 1992-10-15, Last modification date: 2024-12-25) |
| Primary citation | Barford, D.,Johnson, L.N. The allosteric transition of glycogen phosphorylase. Nature, 340:609-616, 1989 Cited by PubMed 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. PubMed: 2770867DOI: 10.1038/340609a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
Download full validation report
