Preliminary crystallographic characterization of an RNA helicase from Kunjin virus

Journal Article · Fri Sep 01 04:00:00 EDT 2006 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309106028776· OSTI ID:22356435

Mastrangelo, Eloise; Bollati, Michela; Milani, Mario ^[1]; Brisbarre, Nadège; Lamballerie, Xavier de ^[2]; Coutard, Bruno; Canard, Bruno ^[3]; Khromykh, Alexander ^[4]; Bolognesi, Martino ^[1]

---

1. Department of Biomolecular Sciences and Biotechnology, CNR-INFM, University of Milano, Via Celoria 26, 20133 Milano (Italy)
2. Unité des Virus Emergents, Faculté de Médecine, 27 Boulevard Jean Moulin, 13005 Marseille (France)
3. Laboratoire Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS ESIL, Case 932, 163 Avenue de Luminy, 13288 Marseille CEDEX 9 (France)
4. RNA Virology Laboratory, School of Molecular and Microbial Sciences, The University of Queensland, Brisbane, QLD 4072 (Australia)

The C-terminal 440 amino acids of the NS3 protein from Kunjin virus (Flaviviridae) code for a helicase. The protein has been overexpressed and crystallized. Characterization of the isolated monoclinic crystal form and diffraction data (at 3.0 Å resolution) are presented, together with a preliminary molecular-replacement solution. Kunjin virus is a member of the Flavivirus genus and is an Australian variant of West Nile virus. The C-terminal domain of the Kunjin virus NS3 protein displays helicase activity. The protein is thought to separate daughter and template RNA strands, assisting the initiation of replication by unwinding RNA secondary structure in the 3′ nontranslated region. Expression, purification and preliminary crystallographic characterization of the NS3 helicase domain are reported. It is shown that Kunjin virus helicase may adopt a dimeric assembly in absence of nucleic acids, oligomerization being a means to provide the helicases with multiple nucleic acid-binding capability, facilitating translocation along the RNA strands. Kunjin virus NS3 helicase domain is an attractive model for studying the molecular mechanisms of flavivirus replication, while simultaneously providing a new basis for the rational development of anti-flaviviral compounds.

• OSTI ID: 22356435
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 9 Vol. 62; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALS
DIFFRACTION
MATHEMATICAL SOLUTIONS
RESOLUTION
SOLUTIONS
TRANSLOCATION