title: The crystal structure of D212 from sulfolobus spindle-shaped virus ragged hills reveals a new member of the PD-(D/E)XK nuclease superfamily.
abstract: 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.
authors.affiliation: Thermal Biology Institute, Montana State University, Bozeman, MT 59717, USA.
authors.forename: Smita K
authors.initials: SK
authors.lastname: Menon
authors.forename: Brian J
authors.initials: BJ
authors.lastname: Eilers
authors.forename: Mark J
authors.initials: MJ
authors.lastname: Young
authors.forename: C Martin
authors.initials: CM
authors.lastname: Lawrence
mesh_terms: D000595:Amino Acid Sequence; D003851:Deoxyribonucleases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D019241:Fuselloviridae / Q000737:chemistry / Q000145:classification / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D005810:Multigene Family; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D014764:Viral Proteins; D003851:Deoxyribonucleases