6QV3

Crystal structure of the Ski2 RNA-helicase Brr2 from Chaetomium thermophilum bound to ADP

Summary for 6QV3

• Entry DOI: 10.2210/pdb6qv3/pdb
• Descriptor: Pre-mRNA splicing helicase-like protein, ADENOSINE-5'-DIPHOSPHATE, MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: helicase adp brr2 ski2 chaetomium thermophilum splicing rna, rna binding protein
• Biological source: Chaetomium thermophilum
• Total number of polymer chains: 1
• Total formula weight: 197939.97

Authors

Absmeier, E.,Santos, K.F.,Wahl, M.C. (deposition date: 2019-03-01, release date: 2020-01-15, Last modification date: 2024-01-24)

Primary citation

Absmeier, E.,Santos, K.F.,Wahl, M.C.
Molecular Mechanism Underlying Inhibition of Intrinsic ATPase Activity in a Ski2-like RNA Helicase.
Structure, 28:236-243.e3, 2020

PubMed Abstract: 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 ATPγS-bound states, revealing nucleotide-induced conformational changes and a hitherto unknown ATPγS 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.

PubMed: 31859026
DOI: 10.1016/j.str.2019.11.014

Experimental method

X-RAY DIFFRACTION (2.9 Å)