Crystal structure of a DExx box DNA helicase

Abstract

THERE are a wide variety of helicases that unwind helical DNA¹ and RNA substrates². The twelve helicases that have been identified in Escherichia coli¹ play a role in almost all cellular processes involving nucleic acids. We have solved the crystal structure of a monomeric form of a DNA helicase from Bacillus stearothermo-philus, alone and in a complex with ADP, at 2.5 and 2.9 Å resolution, respectively. The enzyme comprises two domains with a deep cleft running between them. The ATP-binding site, which is situated at the bottom of this cleft, is formed by motifs that are conserved across the superfamily of related helicases. Unexpected structural homo logy with the DNA recombination protein, RecA, suggests how ATP binding and hydrolysis may drive conformational changes of the enzyme during catalysis, and implies that there is a common mechanism for all helicases.