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

Panos Soultanas

doi:10.1016/j.str.2005.04.006

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

Panos Soultanas

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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.

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Amino Acid Sequence Binding Sites Conserved Sequence DNA Helicases DNA Primase Escherichia coli Evolution, Molecular Geobacillus stearothermophilus Models, Molecular Protein Conformation Protein Structure, Tertiary Structure-Activity Relationship Journal Article Research Support, Non-U.S. Gov't Review

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Panos Soultanas. 2005. The bacterial helicase-primase interaction: a common structural/functional module.. https://doi.org/10.1016/j.str.2005.04.006

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