9DU5
Cryo-EM structure of phosphoglucomutase from Thermococcus kodakarensis
Summary for 9DU5
| Entry DOI | 10.2210/pdb9du5/pdb |
| EMDB information | 47167 |
| Descriptor | Phosphoglucomutase/phosphomannomutase (1 entity in total) |
| Functional Keywords | isomerase, phosphotransferase activity, glycogen metabolism, thermococcus kodakarensis |
| Biological source | Thermococcus kodakarensis |
| Total number of polymer chains | 4 |
| Total formula weight | 199688.19 |
| Authors | Naz, Z.,Rathore, I.,Saleem, M.,Rahman, M.,Rashid, N.,Wlodawer, A. (deposition date: 2024-10-02, release date: 2025-04-16) |
| Primary citation | Naz, Z.,Rathore, I.,Saleem, M.,Rahman, M.,Wlodawer, A.,Rashid, N. A Bifunctional Phosphoglucomutase/Phosphomannomutase from Thermococcus kodakarensis : Biophysical Analysis and Cryo-EM Structure. Biomolecules, 15:-, 2025 Cited by PubMed Abstract: Phosphoglucomutase (EC 5.4.2.2., PGM), a key enzyme of glycogenolysis and glycogenesis, catalyzes the interconversion of glucose 1-phosphate and glucose 6-phosphate, whereas phosphomannomutase (EC 5.4.2.8., PMM) transfers the phosphate group from the 1' to the 6', or from the 6' to the 1' position in mannose phosphate. However, in the hyperthermophilic archaeon , a single gene, , encodes a protein with both PGM and PMM activities. Here, we report biophysical analysis and the 2.45 Å resolution cryo-EM structure of this novel enzyme. Our results demonstrate a specific arrangement of the four subunits in the quaternary structure, displaying a distinct catalytic cleft required for the bifunctional activity at extremely high temperatures. To the best of our knowledge, this is the first biophysical characterization and cryo-EM structure elucidation of a thermostable, bifunctional PGM/PMM. PubMed: 40149855DOI: 10.3390/biom15030319 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.45 Å) |
Structure validation
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