3FHD

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

3FHD の概要

• エントリーDOI: 10.2210/pdb3fhd/pdb
• 分子名称: ORF 37, SULFATE ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: enase like pd-(d/e)xk superfamily, hydrolase
• 由来する生物種: Human herpesvirus 8 type M (Kaposi's sarcoma-associated herpesvirus)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57937.02

構造登録者

Dahlroth, S.L.,Gurmu, D.,Schmitzberger, F.,Haas, J.,Erlandsen, H.,Nordlund, P. (登録日: 2008-12-09, 公開日: 2009-11-24, 最終更新日: 2024-03-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.85 Å)