Communications Biology (Jan 2022)

Cooperative allostery and structural dynamics of streptavidin at cryogenic- and ambient-temperature

  • Esra Ayan,
  • Busra Yuksel,
  • Ebru Destan,
  • Fatma Betul Ertem,
  • Gunseli Yildirim,
  • Meryem Eren,
  • Oleksandr M. Yefanov,
  • Anton Barty,
  • Alexandra Tolstikova,
  • Gihan K. Ketawala,
  • Sabine Botha,
  • E. Han Dao,
  • Brandon Hayes,
  • Mengning Liang,
  • Matthew H. Seaberg,
  • Mark S. Hunter,
  • Alexander Batyuk,
  • Valerio Mariani,
  • Zhen Su,
  • Frederic Poitevin,
  • Chun Hong Yoon,
  • Christopher Kupitz,
  • Aina Cohen,
  • Tzanko Doukov,
  • Raymond G. Sierra,
  • Çağdaş Dağ,
  • Hasan DeMirci

DOI
https://doi.org/10.1038/s42003-021-02903-7
Journal volume & issue
Vol. 5, no. 1
pp. 1 – 13

Abstract

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Ayan et al. report two structures of the protein streptavidin - one at ambient temperature determined using serial femtosecond crystallography and a second one determined at cryogenic temperature. These results provide insights into the structural dynamics of apo streptavidin and reveal a cooperative allostery between monomers for binding to biotin, and the findings are supported by GNM analysis.