Panos Soultanas
The bacterial helicase-primase interaction: a common structural/functional module
Soultanas, Panos
Authors
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), https://doi.org/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 | 1878-4186 |
Publisher | Elsevier |
Peer Reviewed | Peer Reviewed |
Volume | 13 |
Issue | 6 |
DOI | https://doi.org/10.1016/j.str.2005.04.006 |
Public URL | https://nottingham-repository.worktribe.com/output/1019962 |
Publisher URL | http://www.elsevier.com/wps/find/journaldescription.cws_home/622315/description#description |
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