Open AccessThe Crystal Structure of D212 from Sulfolobus Spindle-Shaped Virus Ragged Hills Reveals a New Member of the PD-(D/E)XK Nuclease Superfamily
Author(s) -
Smita Me,
Brian J. Eilers,
Mark Young,
C. Martin Lawrence
Publication year - 2010
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.01663-09
Subject(s) - biology , sulfolobus , nuclease , superfamily , virology , microbiology and biotechnology , genetics , dna , archaea , gene
Structural studies have made significant contributions to our understanding ofSulfolobus spindle-shaped viruses (Fuselloviridae ), an important model system for archaeal viruses. Continuing these efforts, we report the structure of D212 fromSulfolobus 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.