The bacterial helicase-primase interaction: a common structural/functional module.

ABSTRACT: The lack of a high-resolution structure for the bacterial helicase-primase complex and the fragmented structural information for the individual proteins have been hindering our detailed understanding of this crucial binary protein interaction. Two new structures for the helicase-interacting domain of the bacterial primases from Escherichia coli and Bacillus stearothermophilus have recently been solved and both revealed a unique and surprising structural similarity to the amino-terminal domain of the helicase itself. In this minireview, the current data are discussed and important new structural and functional aspects of the helicase-primase interaction are highlighted. An attractive structural model with direct biological significance for the function of this complex and also for the devel

SUBMITTER: Soultanas P 

PROVIDER: S-EPMC3033576 | biostudies-literature | 2005 Jun

REPOSITORIES: biostudies-literature