Nature Communications (Dec 2020)

A substrate binding model for the KEOPS tRNA modifying complex

  • Jonah Beenstock,
  • Samara Mishelle Ona,
  • Jennifer Porat,
  • Stephen Orlicky,
  • Leo C. K. Wan,
  • Derek F. Ceccarelli,
  • Pierre Maisonneuve,
  • Rachel K. Szilard,
  • Zhe Yin,
  • Dheva Setiaputra,
  • Daniel Y. L. Mao,
  • Morgan Khan,
  • Shaunak Raval,
  • David C. Schriemer,
  • Mark A. Bayfield,
  • Daniel Durocher,
  • Frank Sicheri

DOI
https://doi.org/10.1038/s41467-020-19990-5
Journal volume & issue
Vol. 11, no. 1
pp. 1 – 17

Abstract

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KEOPS is an evolutionary conserved complex with a core of four core subunits—Pcc1, Kae1, Bud32 and Cgi121—that catalyzes the universal and essential tRNA modification N6-threonylcarbamoyl adenosine (t6A). Here the authors describe a Cgi121-tRNA crystal structure and new composite model of the KEOPS holo-enzyme-substrate complex that shed light on the t6A catalytic cycle and its regulation.