Anno2012
AutoriMastrangelo E; Bolognesi M; Milani M
AbstractMotor 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.
RivistaBiochemical And Biophysical Research Communications
ISSN0006-291X
Impact factor
Volume417
Pagina inizio87
Pagina fine84
Autori IBFEloise MASTRANGELO, Mario MILANI, Martino BOLOGNESI
Linee di Ricerca IBFMD.P01.005.001
Sedi IBFIBF.MI