Purification, crystallization and preliminary X-ray diffraction studies of the archaeal virus resolvase SIRV2.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 61(Pt 5): 507-9, 2005 May 01.
Article
em En
| MEDLINE
| ID: mdl-16511081
ABSTRACT
The Holliday junction (or four-way junction) is the universal DNA intermediate whose interaction with resolving proteins is one of the major events in the recombinational process. These proteins, called DNA junction-resolving enzymes or resolvases, bind to the junction and catalyse DNA cleavage, promoting the release of two DNA duplexes. SIRV2 Hjc, a viral resolvase infecting a thermophylic archaeon, has been cloned, expressed and purified. Crystals have been obtained in space group C2, with unit-cell parameters a = 147.8, b = 99.9, c = 87.6, beta = 109.46 degrees, and a full data set has been collected at 3.4 A resolution. The self-rotation function indicates the presence of two dimers in the asymmetric unit and a high solvent content (77%). Molecular-replacement trials using known similar resolvase structures have so far been unsuccessful, indicating possible significant structural rearrangements.
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Base de dados:
MEDLINE
Assunto principal:
Vírus de Archaea
/
Rudiviridae
/
Resolvases de Junção Holliday
Idioma:
En
Ano de publicação:
2005
Tipo de documento:
Article