9du5
From Proteopedia
Cryo-EM structure of phosphoglucomutase from Thermococcus kodakarensis
Structural highlights
FunctionPGMMM_THEKO Catalyzes the interconversion of glucose 1-phosphate and glucose 6-phosphate, and the interconversion of mannose 1-phosphate and mannose 6-phosphate. Also displays low activity with deoxyribose 1-phosphate and glucosamine 1-phosphate.[1] Publication Abstract from PubMedPhosphoglucomutase (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 Thermococcus kodakarensis, a single gene, Tk1108, encodes a protein with both PGM and PMM activities. Here, we report biophysical analysis and the 2.45 A 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. A Bifunctional Phosphoglucomutase/Phosphomannomutase from Thermococcus kodakarensis: Biophysical Analysis and Cryo-EM Structure.,Naz Z, Rathore I, Saleem M, Rahman M, Wlodawer A, Rashid N Biomolecules. 2025 Feb 21;15(3):319. doi: 10.3390/biom15030319. PMID:40149855[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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