Nature Communications (Nov 2020)

Structural insights into the mechanism of rhodopsin phosphodiesterase

  • Tatsuya Ikuta,
  • Wataru Shihoya,
  • Masahiro Sugiura,
  • Kazuho Yoshida,
  • Masahito Watari,
  • Takaya Tokano,
  • Keitaro Yamashita,
  • Kota Katayama,
  • Satoshi P. Tsunoda,
  • Takayuki Uchihashi,
  • Hideki Kandori,
  • Osamu Nureki

DOI
https://doi.org/10.1038/s41467-020-19376-7
Journal volume & issue
Vol. 11, no. 1
pp. 1 – 12

Abstract

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Rhodopsin phosphodiesterase (Rh-PDE) hydrolyzes both cAMP and cGMP in a light-dependent manner. Structural and functional analyses of the Rh-PDE from Salpingoeca rosetta reveal unusual rhodopsin topology comprising 8 transmembrane helices (TMs) and suggest that TM0 plays a crucial role in the enzymatic photoactivity.