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

By Panos Soultanas

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 development of new antibacterial compounds is examined

Publisher: Elsevier
Year: 2005
OAI identifier: oai:eprints.nottingham.ac.uk:1106
Provided by: Nottingham ePrints

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