| Literature DB >> 15939015 |
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.Entities:
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Year: 2005 PMID: 15939015 PMCID: PMC3033576 DOI: 10.1016/j.str.2005.04.006
Source DB: PubMed Journal: Structure ISSN: 0969-2126 Impact factor: 5.006