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(15): 8309-13, 2012 Aug.
Article
in En
| MEDLINE
| ID: mdl-22593158
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Viral Proteins
/
Evolution, Molecular
/
Integrases
/
Archaeal Viruses
Language:
En
Journal:
J Virol
Year:
2012
Type:
Article
Affiliation country:
United States