Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein.

Together with the NS5 polymerase, the NS3 helicase has a pivotal function in flavivirus RNA replication and constitutes an important drug target. We captured the dengue virus NS3 helicase at several stages along the catalytic pathway including bound to single-stranded (ss) RNA, to an ATP analogue, to a transition-state analogue and to ATP hydrolysis products. RNA recognition appears largely sequence independent in a way remarkably similar to eukaryotic DEAD box proteins Vasa and eIF4AIII.

The last five amino acid residues at the C-terminus of PRK1/PKN is essential for full lipid responsiveness.

PRK1/PKN is a member of the protein kinase C (PKC) superfamily of serine/threonine protein kinases. Despite its important role as a RhoA effector, limited information is available regarding how this kinase is regulated. We show here that the last seven amino acid residues at the C-terminus is dispensable for the catalytic activity of PRK1 but is critical for the in vivo stability of this kinase.

Structure, crystal packing and molecular dynamics of the calponin-homology domain of Schizosaccharomyces pombe Rng2.

Schizosaccharomyces pombe Rng2 is an IQGAP protein that is essential for the assembly of an actomyosin ring during cytokinesis. Rng2 contains an amino-terminal calponin-homology (CH) domain, 11 IQ repeats and a RasGAP-homology domain. CH domains are known mainly for their ability to bind F-actin, although they have other ligands in vivo and there are only few examples of actin-binding single CH domains.

Expression, purification, crystallization and preliminary crystallographic analysis of the calponin-homology domain of Rng2.

Rng2 is a multidomain protein component of the actiomyosin ring and the spindle pole body necessary for cytokinesis in Schizosaccharomyces pombe. The calponin-homology domain of Rng2 from S. pombe has been overexpressed, purified and crystallized.