Structural highlights
Publication Abstract from PubMed
Structural studies have made significant contributions to our understanding of Sulfolobus spindle-shaped viruses (Fuselloviridae), an important model system for archaeal viruses. Continuing these efforts, we report the structure of D212 from Sulfolobus spindle-shaped virus Ragged Hills. The overall fold and conservation of active site residues place D212 in the PD-(D/E)XK nuclease superfamily. The greatest structural similarity is found to the archaeal Holliday junction cleavage enzymes, strongly suggesting a role in DNA replication, repair, or recombination. Other roles associated with nuclease activity are also considered.
The crystal structure of D212 from sulfolobus spindle-shaped virus ragged hills reveals a new member of the PD-(D/E)XK nuclease superfamily.,Menon SK, Eilers BJ, Young MJ, Lawrence CM J Virol. 2010 Jun;84(12):5890-7. Epub 2010 Apr 7. PMID:20375162[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Menon SK, Eilers BJ, Young MJ, Lawrence CM. The crystal structure of D212 from sulfolobus spindle-shaped virus ragged hills reveals a new member of the PD-(D/E)XK nuclease superfamily. J Virol. 2010 Jun;84(12):5890-7. Epub 2010 Apr 7. PMID:20375162 doi:10.1128/JVI.01663-09
