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M. mazei glutamine synthetase and glutamine synthetase-GlnK1 structures reveal enzyme regulation by oligomer modulation

Author

Listed:
  • Maria A. Schumacher

    (Duke University Medical Center)

  • Raul Salinas

    (Duke University Medical Center)

  • Brady A. Travis

    (Duke University Medical Center)

  • Rajiv Ranjan Singh

    (Duke University Medical Center)

  • Nicholas Lent

    (Duke University Medical Center)

Abstract

Glutamine synthetases (GS) play central roles in cellular nitrogen assimilation. Although GS active-site formation requires the oligomerization of just two GS subunits, all GS form large, multi-oligomeric machines. Here we describe a structural dissection of the archaeal Methanosarcina mazei (Mm) GS and its regulation. We show that Mm GS forms unstable dodecamers. Strikingly, we show this Mm GS oligomerization property is leveraged for a unique mode of regulation whereby labile Mm GS hexamers are stabilized by binding the nitrogen regulatory protein, GlnK1. Our GS-GlnK1 structure shows that GlnK1 functions as molecular glue to affix GS hexamers together, stabilizing formation of GS active-sites. These data, therefore, reveal the structural basis for a unique form of enzyme regulation by oligomer modulation.

Suggested Citation

  • Maria A. Schumacher & Raul Salinas & Brady A. Travis & Rajiv Ranjan Singh & Nicholas Lent, 2023. "M. mazei glutamine synthetase and glutamine synthetase-GlnK1 structures reveal enzyme regulation by oligomer modulation," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-43243-w
    DOI: 10.1038/s41467-023-43243-w
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    References listed on IDEAS

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    1. Brady A. Travis & Jared V. Peck & Raul Salinas & Brandon Dopkins & Nicholas Lent & Viet D. Nguyen & Mario J. Borgnia & Richard G. Brennan & Maria A. Schumacher, 2022. "Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
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