3UXU

The structure of the catalytic domain of the Sulfolobus Spindle-shaped viral integrase reveals an evolutionarily conserved catalytic core and supports a mechanism of DNA cleavage in trans

Summary for 3UXU

Entry DOI	10.2210/pdb3uxu/pdb
Descriptor	Probable integrase, PHOSPHATE ION (3 entities in total)
Functional Keywords	ssv1, archaea, archaeal virus, hyperthermophilic, integrase, disulfide, recombination
Biological source	Sulfolobus virus 1
Total number of polymer chains	1
Total formula weight	20116.22
Authors	Eilers, B.J.,Young, M.J.,Lawrence, C.M. (deposition date: 2011-12-05, release date: 2012-05-16, Last modification date: 2024-10-16)
Primary citation	Eilers, B.J.,Young, M.J.,Lawrence, C.M. The Structure of an Archaeal Viral Integrase Reveals an Evolutionarily Conserved Catalytic Core yet Supports a Mechanism of DNA Cleavage in trans. J.Virol., 86:8309-8313, 2012 Cited by PubMed 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. PubMed: 22593158 DOI: 10.1128/JVI.00547-12 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.706 Å)

Structure validation