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

Soultanas, Panos

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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.

Citation

Soultanas, P. (2005). The bacterial helicase-primase interaction: a common structural/functional module. Structure, 13(6), doi:10.1016/j.str.2005.04.006

Journal Article Type Article
Publication Date Jun 1, 2005
Deposit Date Aug 14, 2009
Publicly Available Date Aug 14, 2009
Journal Structure
Print ISSN 0969-2126
Electronic ISSN 0969-2126
Publisher Elsevier
Peer Reviewed Peer Reviewed
Volume 13
Issue 6
DOI https://doi.org/10.1016/j.str.2005.04.006
Public URL http://eprints.nottingham.ac.uk/id/eprint/1106
Publisher URL http://www.elsevier.com/wps/find/journaldescription.cws_home/622315/description#description
Copyright Statement Copyright information regarding this work can be found at the following address: http://eprints.nottingham.ac.uk/end_user_agreement.pdf

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Copyright Statement
Copyright information regarding this work can be found at the following address: http://eprints.nottingham.ac.uk/end_user_agreement.pdf





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