Structure of Hexameric DnaB Helicase and Its Complex with a Domain of DnaG Primase-Reference-Cited by-同舟云学术

Structure of Hexameric DnaB Helicase and Its Complex with a Domain of DnaG Primase

Published:2007-10-19 Issue:5849 Volume:318 Page:459-463
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Bailey Scott¹²,Eliason William K.¹²,Steitz Thomas A.¹²

Affiliation:

1. Department of Molecular Biophysics and Biochemistry and Howard Hughes Medical Institute, Yale University, New Haven, CT 06520, USA.

2. Department of Chemistry, Yale University, New Haven, CT 06520, USA.

Abstract

The complex between the DnaB helicase and the DnaG primase unwinds duplex DNA at the eubacterial replication fork and synthesizes the Okazaki RNA primers. The crystal structures of hexameric DnaB and its complex with the helicase binding domain (HBD) of DnaG reveal that within the hexamer the two domains of DnaB pack with strikingly different symmetries to form a distinct two-layered ring structure. Each of three bound HBDs stabilizes the DnaB hexamer in a conformation that may increase its processivity. Three positive, conserved electrostatic patches on the N-terminal domain of DnaB may also serve as a binding site for DNA and thereby guide the DNA to a DnaG active site.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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