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.

Preliminary crystallographic characterization of an RNA helicase from Kunjin virus / E. Mastrangelo, M. Bollati, M. Milani, N. Brisbarre, X. de Lamballerie, B. Coutard, B. Canard, A. Khromykh, M. Bolognesi. - In: ACTA CRYSTALLOGRAPHICA. SECTION F, STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS. - ISSN 1744-3091. - 62:9(2006 Sep), pp. 876-879.

Preliminary crystallographic characterization of an RNA helicase from Kunjin virus

E. Mastrangelo;M. Bollati;M. Bolognesi
2006-09

Abstract

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.
Enzymes Role: BSU (Biological study, unclassified) ; PEP (Physical, engineering or chemical process) ; PRP (Properties) ; PYP (Physical process) ; BIOL (Biological study) ; PROC (Process) (RNA helicase ; crystn. and preliminary x-ray anal. of RNA helicase of Kunjin virus) ; Kunjin virus (crystn. and preliminary x-ray anal. of RNA helicase of Kunjin virus) ; Crystal growth ; Crystal structure (of RNA helicase of Kunjin virus) ; crystal-structure ; light-scattering ; mechanism ; proteins ; binding
Settore BIO/10 - Biochimica
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2434/62740
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