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A Bifunctional Phosphoglucomutase/Phosphomannomutase from Thermococcus kodakarensis: Biophysical Analysis and Cryo-EM Structure

  1. Author:
    Naz, Zahra [ORCID]
    Rathore, Ishan [ORCID]
    Saleem, Muhammad [ORCID]
    Rahman, Moazur
    Wlodawer,Alexander [ORCID]
    Rashid, Naeem [ORCID]

  2. Author Address

    School of Biological Sciences, University of the Punjab, Lahore 54590, Pakistan., Center for Structural Biology, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA.,
    1. Year: 2025
    2. Date: Feb 21
    3. Epub Date: 2025 02 21
  2. Journal: Biomolecules
    1. 15
    2. 3
  4. Type of Article: Article
  5. Article Number: 319
  1. 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 39; to the 6 39;, or from the 6 39; to the 1 39; 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 2.45 197; 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.

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External Sources

  1. View Full Text
  2. DOI: 10.3390/biom15030319
  3. PMID: 40149855
  4. PMCID: PMC11940775
  5. PII : biom15030319

Library Notes

  1. Fiscal Year: FY2024-2025
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