Summary for 7P7D
| Entry DOI | 10.2210/pdb7p7d/pdb |
| Related | 1GPB |
| Descriptor | Glycogen phosphorylase, muscle form, DIMETHYL SULFOXIDE (3 entities in total) |
| Functional Keywords | glycogen metabolism, transferase |
| Biological source | Oryctolagus cuniculus (Rabbit) |
| Total number of polymer chains | 1 |
| Total formula weight | 97838.63 |
| Authors | Stravodimos, G.A.,Leonidas, D.D. (deposition date: 2021-07-19, release date: 2021-07-28, Last modification date: 2024-01-31) |
| Primary citation | Leonidas, D.D.,Zographos, S.E.,Tsitsanou, K.E.,Skamnaki, V.T.,Stravodimos, G.,Kyriakis, E. Glycogen phosphorylase revisited: extending the resolution of the R- and T-state structures of the free enzyme and in complex with allosteric activators. Acta Crystallogr.,Sect.F, 77:303-311, 2021 Cited by PubMed Abstract: The crystal structures of free T-state and R-state glycogen phosphorylase (GP) and of R-state GP in complex with the allosteric activators IMP and AMP are reported at improved resolution. GP is a validated pharmaceutical target for the development of antihyperglycaemic agents, and the reported structures may have a significant impact on structure-based drug-design efforts. Comparisons with previously reported structures at lower resolution reveal the detailed conformation of important structural features in the allosteric transition of GP from the T-state to the R-state. The conformation of the N-terminal segment (residues 7-17), the position of which was not located in previous T-state structures, was revealed to form an α-helix (now termed α0). The conformation of this segment (which contains Ser14, phosphorylation of which leads to the activation of GP) is significantly different between the T-state and the R-state, pointing in opposite directions. In the T-state it is packed between helices α4 and α16 (residues 104-115 and 497-508, respectively), while in the R-state it is packed against helix α1 (residues 22'-38') and towards the loop connecting helices α4' and α5' of the neighbouring subunit. The allosteric binding site where AMP and IMP bind is formed by the ordering of a loop (residues 313-326) which is disordered in the free structure, and adopts a conformation dictated mainly by the type of nucleotide that binds at this site. PubMed: 34473107DOI: 10.1107/S2053230X21008542 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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