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Literature DB >> 32023430

Closing in on ATPase Activity by an RNA Helicase.

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.

Entities: Chemical Gene

Mesh：

Substances：

Year: 2020 PMID： 32023430 PMCID： PMC8243761 DOI： 10.1016/j.str.2020.01.007

Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006

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References

10 in total

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4. The crystal structure of S. cerevisiae Ski2, a DExH helicase associated with the cytoplasmic functions of the exosome.

Authors: Felix Halbach; Michaela Rode; Elena Conti
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Closing in on ATPase Activity by an RNA Helicase.

Review 1. SF1 and SF2 helicases: family matters.

Review 2. Ski2-like RNA helicase structures: common themes and complex assemblies.

3. Structure of the nuclear exosome captured on a maturing preribosome.

4. The crystal structure of S. cerevisiae Ski2, a DExH helicase associated with the cytoplasmic functions of the exosome.

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

6. The yeast ski complex: crystal structure and RNA channeling to the exosome complex.

7. Helicase-Dependent RNA Decay Illuminated by a Cryo-EM Structure of a Human Nuclear RNA Exosome-MTR4 Complex.

8. The large N-terminal region of the Brr2 RNA helicase guides productive spliceosome activation.

9. Structural insights into the mechanism of the DEAH-box RNA helicase Prp43.

10. Cryo-EM structure of the yeast U4/U6.U5 tri-snRNP at 3.7 Å resolution.