2.7 Å cryo-EM structure of rotavirus core protein VP3, a unique capping machine with a helicase activity-Reference-Cited by-同舟云学术

2.7 Å cryo-EM structure of rotavirus core protein VP3, a unique capping machine with a helicase activity

Published:2020-04-17 Issue:16 Volume:6 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Kumar Dilip¹^ORCID,Yu Xinzhe¹^ORCID,Crawford Sue E.²^ORCID,Moreno Rodolfo¹^ORCID,Jakana Joanita¹³^ORCID,Sankaran Banumathi⁴^ORCID,Anish Ramakrishnan¹^ORCID,Kaundal Soni¹^ORCID,Hu Liya¹^ORCID,Estes Mary K²⁵^ORCID,Wang Zhao¹³⁶^ORCID,Prasad B. V. Venkataram¹²^ORCID

Affiliation:

1. Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.

2. Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX 77030, USA.

3. CryoEM Core, Baylor College of Medicine, Houston, TX 77030, USA.

4. Molecular Biophysics and Integrated Bioimaging, Berkeley Center for Structural Biology, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.

5. Department of Medicine, Baylor College of Medicine, Houston, TX 77030, USA.

6. Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USA.

Abstract

Rotavirus capping enzyme VP3 is a stable tetramer with unique RNA binding, RTPase, and RNA helicase activities.

Funder

National Institutes of Health

U.S. Department of Energy

National Institute of Allergy and Infectious Diseases

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary