3FHD

Crystal structure of the Shutoff and Exonuclease Protein from Kaposis Sarcoma Associated Herpesvirus

Summary for 3FHD

• Entry DOI: 10.2210/pdb3fhd/pdb
• Descriptor: ORF 37, SULFATE ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: enase like pd-(d/e)xk superfamily, hydrolase
• Biological source: Human herpesvirus 8 type M (Kaposi's sarcoma-associated herpesvirus)
• Total number of polymer chains: 1
• Total formula weight: 57937.02

Authors

Dahlroth, S.L.,Gurmu, D.,Schmitzberger, F.,Haas, J.,Erlandsen, H.,Nordlund, P. (deposition date: 2008-12-09, release date: 2009-11-24, Last modification date: 2024-03-20)

Primary citation

Dahlroth, S.L.,Gurmu, D.,Schmitzberger, F.,Engman, H.,Haas, J.,Erlandsen, H.,Nordlund, P.
Crystal structure of the shutoff and exonuclease protein from the oncogenic Kaposi's sarcoma-associated herpesvirus
Febs J., 276:6636-6645, 2009

PubMed Abstract: The Kaposi's sarcoma-associated herpesvirus protein SOX (shut off and exonuclease) and its Epstein-Barr virus homolog, BGLF5, are active during the early lytic phase and belong to the alkaline nuclease family. Both proteins have been shown to be bifunctional, being responsible for DNA maturation as well as host shutoff at the mRNA level. We present the crystal structure of SOX determined at 1.85 A resolution. By modeling DNA binding, we have identified catalytic residues that explain the preferred 5'-exonuclease activity of the alkaline nucleases. The presence of a crevice suitable for binding duplex DNA supports a role for herpes alkaline nucleases in recombination events preceding packaging of viral DNA. Direct interaction with dsDNA is supported by oligonucleotide binding data. Mutations specifically affecting host shutoff map to a surface region of the N-terminal domain, implying an essential role in protein-protein interactions, and link the RNase activity of the enzyme to mRNA degradation pathways.

PubMed: 19843164
DOI: 10.1111/j.1742-4658.2009.07374.x

Experimental method

X-RAY DIFFRACTION (1.85 Å)