Motor proteins are involved in crucial cell activities, such as cargo transport or nucleic acid remodeling, by converting the free energy of ATP hydrolysis into motion or mechanical work. Flavivirus helicase is a motor protein involved in dsRNA separation during viral replication, thus essential for virus infection. Since a clear vision of the protein activity, in particular of the relationship between ATP cycling and dynamics, is missing, we carried over a molecular dynamics study on Dengue virus helicase in its ATP bound and unbound states. Our simulations show different opening levels of the ssRNA access site to the helicase core. Specifically, we show that ATP induces a closed state into the ssRNA access site, likely involved in the helicase unwinding activity.
Flaviviral helicase: Insights into the mechanism of action of a motor protein / E. Mastrangelo, M. Bolognesi, M. Milani. - In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. - ISSN 0006-291X. - 417:1(2012), pp. 84-87.
|Titolo:||Flaviviral helicase: Insights into the mechanism of action of a motor protein|
MASTRANGELO, ELOISE (Primo)
BOLOGNESI, MARTINO (Secondo)
|Parole Chiave:||ATP binding; Flavivirus helicase; Molecular dynamics simulation; Motor protein; Protein structural transitions; RNA remodeling|
|Settore Scientifico Disciplinare:||Settore BIO/10 - Biochimica|
|Progetto:||Small-molecule Inhibitor Leads Versus emerging and neglected RNA viruses|
|Data di pubblicazione:||2012|
|Digital Object Identifier (DOI):||http://dx.doi.org/10.1016/j.bbrc.2011.11.060|
|Appare nelle tipologie:||01 - Articolo su periodico|