6O3V

Crystal structure for RVA-VP3

Summary for 6O3V

• Entry DOI: 10.2210/pdb6o3v/pdb
• Descriptor: Protein VP3, GUANOSINE-5'-MONOPHOSPHATE, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: rotavirus, vp3, capping enzyme, guanylyl transferase, methyl transferase, rtpase, pde, structural protein
• Biological source: Rotavirus A
• Total number of polymer chains: 3
• Total formula weight: 294675.52

Authors

Kumar, D.,Yu, X.,Wang, Z.,Hu, L.,Prasad, V. (deposition date: 2019-02-27, release date: 2020-03-04, Last modification date: 2024-03-13)

Primary citation

Kumar, D.,Yu, X.,Crawford, S.E.,Moreno, R.,Jakana, J.,Sankaran, B.,Anish, R.,Kaundal, S.,Hu, L.,Estes, M.K.,Wang, Z.,Prasad, B.V.V.
2.7 angstrom cryo-EM structure of rotavirus core protein VP3, a unique capping machine with a helicase activity.
Sci Adv, 6:eaay6410-eaay6410, 2020

PubMed Abstract: In many viruses, including rotavirus (RV), the major pathogen of infantile gastroenteritis, capping of viral messenger RNAs is a pivotal step for efficient translation of the viral genome. In RV, VP3 caps the nascent transcripts synthesized from the genomic dsRNA segments by the RV polymerase VP1 within the particle core. Here, from cryo-electron microscopy, x-ray crystallography, and biochemical analyses, we show that VP3 forms a stable tetrameric assembly with each subunit having a modular domain organization, which uniquely integrates five distinct enzymatic steps required for capping the transcripts. In addition to the previously known guanylyl- and methyltransferase activities, we show that VP3 exhibits hitherto unsuspected RNA triphosphatase activity necessary for initiating transcript capping and RNA helicase activity likely required for separating the RNA duplex formed transiently during endogenous transcription. From our studies, we propose a new mechanism for how VP3 inside the virion core caps the nascent transcripts exiting from the polymerase.

PubMed: 32494598
DOI: 10.1126/sciadv.aay6410

Experimental method

X-RAY DIFFRACTION (3.5 Å)