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TitleA Bifunctional Phosphoglucomutase/Phosphomannomutase from : Biophysical Analysis and Cryo-EM Structure.
Journal, issue, pagesBiomolecules, Vol. 15, Issue 3, Year 2025
Publish dateFeb 21, 2025
AuthorsZahra Naz / Ishan Rathore / Muhammad Saleem / Moazur Rahman / Alexander Wlodawer / Naeem Rashid /
PubMed AbstractPhosphoglucomutase (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. ...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.
External linksBiomolecules / PubMed:40149855 / PubMed Central
MethodsEM (single particle)
Resolution2.45 Å
Structure data

47167

9du5

EMDB-47167, PDB-9du5:
Cryo-EM structure of phosphoglucomutase from Thermococcus kodakarensis
Method: EM (single particle) / Resolution: 2.45 Å

Source
  • thermococcus kodakarensis (archaea)
KeywordsISOMERASE / phosphotransferase activity / glycogen metabolism / Thermococcus kodakarensis

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