Closing in on ATPase Activity by an RNA Helicase

Sean J Johnson; Matthew K Yim

doi:10.1016/j.str.2020.01.007

Closing in on ATPase Activity by an RNA Helicase

Structure. 2020 Feb 4;28(2):143-144. doi: 10.1016/j.str.2020.01.007.

Authors

Sean J Johnson¹, Matthew K Yim²

Affiliations

¹ Department of Chemistry & Biochemistry, Utah State University, Logan, UH, USA. Electronic address: sean.johnson@usu.edu.
² Department of Chemistry & Biochemistry, Utah State University, Logan, UH, USA.

Abstract

In this issue of Structure, Absmeier et al. (2020) describe the molecular mechanisms employed by an RNA helicase to prevent premature ATP hydrolysis upon nucleotide binding.

Publication types

Research Support, N.I.H., Extramural
Comment

MeSH terms

Adenosine Triphosphatases*
Adenosine Triphosphate
Hydrolysis
RNA Helicases*

Substances

Adenosine Triphosphate
Adenosine Triphosphatases
RNA Helicases

Grants and funding

R01 GM117311/GM/NIGMS NIH HHS/United States