Structural information on helicase proteins has expanded recently beyond the DNA
helicases Rep and PcrA, and the hepatitis C virus RNA helicase to include UvrB, members …

▪ Abstract Helicases are motor proteins that couple the hydrolysis of nucleoside triphosphate
(NTPase) to nucleic acid unwinding. The hexameric helicases have a characteristic ring …

Cryoelectron microscopy of biological molecules is among the hottest growth areas in
biophysics and structural biology at present, and Frank is arguably the most distinguished …

The AAA+ ATPases are enzymes containing a P-loop NTPase domain, and function as
molecular chaperones, ATPase subunits of proteases, helicases or nucleic-acid-stimulated …

The E1 protein of papillomavirus is a hexameric ring helicase belonging to the AAA+ family.
The mechanism that couples the ATP cycle to DNA translocation has been unclear. Here we …

▪ Abstract DNA primases are enzymes whose continual activity is required at the DNA
replication fork. They catalyze the synthesis of short RNA molecules used as primers for …

▪ Abstract The RuvA, RuvB, and RuvC proteins in Escherichia coli play important roles in the
late stages of homologous genetic recombination and the recombinational repair of …

Determining how a protein folds is a central problem in structural biology. The rate of folding
of many proteins is determined by the transition state, so that a knowledge of its structure is …

We have determined the crystal structure of an active, hexameric fragment of the gene 4
helicase from bacteriophage T7. The structure reveals how subunit contacts stabilize the …

The initiation of replication is the central event in the bacterial cell cycle. Cells control the
rate of DNA synthesis by modulating the frequency with which new chains are initiated, like …