title: Crystal structure of the C-terminal 2',5'-phosphodiesterase domain of group A rotavirus protein VP3.
abstract: In response to viral infections, the mammalian innate immune system induces the production of the second messenger 2'-5' oligoadenylate (2-5A) to activate latent ribonuclease L (RNase L) that restricts viral replication and promotes apoptosis. A subset of rotaviruses and coronaviruses encode 2',5'-phosphodiesterase enzymes that hydrolyze 2-5A, thereby inhibiting RNase L activation. We report the crystal structure of the 2',5'-phosphodiesterase domain of group A rotavirus protein VP3 at 1.39 Å resolution. The structure exhibits a 2H phosphoesterase fold and reveals conserved active site residues, providing insights into the mechanism of 2-5A degradation in viral evasion of host innate immunity.
authors.affiliation: Department of Biochemistry, University of Zurich, Zurich, Switzerland.
authors.forename: Tobias
authors.initials: T
authors.lastname: Brandmann
authors.forename: Martin
authors.initials: M
authors.lastname: Jinek
mesh_terms: D036022:Capsid Proteins / Q000737:chemistry*; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010727:Phosphoric Diester Hydrolases / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012401:Rotavirus / Q000201:enzymology*
chemical_list: D036022:Capsid Proteins; C442546:VP3 protein, Rotavirus; D010727:Phosphoric Diester Hydrolases
keywords: 2-5A; 2H phosphoesterase; RNase L; immune evasion; innate immunity; oligoadenylate synthase; phosphodiesterase; rotavirus