Rxivist logo

Molecular Mechanism Underlying Inhibition of Intrinsic ATPase Activity in a Ski2-like RNA Helicase

By Eva Absmeier, Karine F. Santos, Markus C. Wahl

Posted 05 Sep 2019
bioRxiv DOI: 10.1101/758169 (published DOI: 10.1016/j.str.2019.11.014)

RNA-dependent NTPases can act as RNA/RNA-protein remodeling enzymes and typically exhibit low NTPase activity in the absence of RNA/RNA-protein substrates. How futile intrinsic NTP hydrolysis is prevented is frequently not known. The ATPase/RNA helicase Brr2 belongs to the Ski2-like family of nucleic acid-dependent NTPases and is an integral component of the spliceosome. Comprehensive nucleotide binding and hydrolysis studies are not available for a member of the Ski2-like family. We present crystal structures of Chaetomium thermophilum Brr2 in the apo, ADP-bound and ATPyS-bound states, revealing nucleotide-induced conformational changes and a hitherto unknown ATPyS binding mode. Our results in conjunction with Brr2 structures in other molecular contexts reveal multiple molecular mechanisms that contribute to the inhibition of intrinsic ATPase activity, including an N-terminal region that restrains the RecA-like domains in an open conformation and exclusion of an attacking water molecule, and suggest how RNA substrate binding can lead to ATPase stimulation.

Download data

  • Downloaded 157 times
  • Download rankings, all-time:
    • Site-wide: 75,871 out of 88,858
    • In biochemistry: 2,420 out of 2,969
  • Year to date:
    • Site-wide: 64,213 out of 88,858
  • Since beginning of last month:
    • Site-wide: 48,635 out of 88,858

Altmetric data

Downloads over time

Distribution of downloads per paper, site-wide


Sign up for the Rxivist weekly newsletter! (Click here for more details.)