5AF2

Crystal structure of the C-terminal 2',5'-phosphodiesterase domain of group A rotavirus protein VP3

Summary for 5AF2

• Entry DOI: 10.2210/pdb5af2/pdb
• Descriptor: VP3, POLYETHYLENE GLYCOL (N=34), POTASSIUM ION, ... (4 entities in total)
• Functional Keywords: hydrolase, phosphodiesterase, 2-5a, 2h phosphoesterase, rnase l, oligoadenylate synthase, innate immunity, immune evasion
• Biological source: ROTAVIRUS A
• Total number of polymer chains: 4
• Total formula weight: 68606.10

Authors

Brandmann, T.,Jinek, M. (deposition date: 2015-01-16, release date: 2015-03-18, Last modification date: 2024-05-08)

Primary citation

Brandmann, T.,Jinek, M.
Crystal Structure of the C-Terminal 2',5'-Phosphodiesterase Domain of Group a Rotavirus Protein Vp3.
Proteins, 83:997-, 2015

PubMed 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.

PubMed: 25758703
DOI: 10.1002/PROT.24794

Experimental method

X-RAY DIFFRACTION (1.39 Å)