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

Soultanas, Panos (2005) The bacterial helicase-primase interaction: a common structural/functional module. Structure, 13 (6). pp. 839-844. ISSN 0969-2126

[img]
Preview
PDF - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
548Kb

Official URL: http://www.elsevier.com/wps/find/journaldescription.cws_home/622315/description#description

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.

Item Type:Article
Schools/Departments:University of Nottingham UK Campus > Faculty of Science > School of Chemistry
ID Code:1106
Deposited By:Soultanas, Prof Panos
Deposited On:14 Aug 2009 15:03
Last Modified:26 Aug 2014 18:00

Repository Staff Only: item control page