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
3uxu is a 1 chain structure with sequence from Sulfolobus virus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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.
The Structure of an Archaeal Viral Integrase Reveals an Evolutionarily Conserved Catalytic Core yet Supports a Mechanism of DNA Cleavage in trans.,Eilers BJ, Young MJ, Lawrence CM J Virol. 2012 Aug;86(15):8309-13. Epub 2012 May 16. PMID:22593158[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Eilers BJ, Young MJ, Lawrence CM. The Structure of an Archaeal Viral Integrase Reveals an Evolutionarily Conserved Catalytic Core yet Supports a Mechanism of DNA Cleavage in trans. J Virol. 2012 Aug;86(15):8309-13. Epub 2012 May 16. PMID:22593158 doi:10.1128/JVI.00547-12
