title: The structure of an archaeal viral integrase reveals an evolutionarily conserved catalytic core yet supports a mechanism of DNA cleavage in trans.
abstract: The first structure of a catalytic domain from a hyperthermophilic archaeal viral integrase reveals a minimal fold similar to that of bacterial HP1 integrase and defines structural elements conserved across three domains of life. However, structural superposition on bacterial Holliday junction complexes and similarities in the C-terminal tail with that of eukaryotic Flp suggest that the catalytic tyrosine and an additional active-site lysine are delivered to neighboring subunits in trans. An intramolecular disulfide bond contributes significant thermostability in vitro.
authors.affiliation: Thermal Biology Institute, Montana State University, Bozeman, Montana, USA.
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: D023641:Archaeal Viruses / Q000201:enzymology*; D004254:DNA Nucleotidyltransferases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D045566:DNA, Cruciform / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D004279:DNA, Viral / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D004795:Enzyme Stability; D019143:Evolution, Molecular; D019426:Integrases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017434:Protein Structure, Tertiary; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D045566:DNA, Cruciform; D004279:DNA, Viral; D014764:Viral Proteins; D004254:DNA Nucleotidyltransferases; C045119:FLP recombinase; D019426:Integrases