The Bacterial Helicase-Primase Interaction: A Common Structural/Functional Module
Open Access
- 30 June 2005
- Vol. 13 (6) , 839-844
- https://doi.org/10.1016/j.str.2005.04.006
Abstract
No abstract availableKeywords
Funding Information
- Biotechnology and Biological Sciences Research Council (BB/C500579/1)
This publication has 40 references indexed in Scilit:
- Solution Structure of the Helicase-Interaction Domain of the Primase DnaGStructure, 2005
- Crystal and Solution Structures of the Helicase-binding Domain of Escherichia coli PrimaseJournal of Biological Chemistry, 2005
- Protein-Protein InteractionsStructure, 2004
- Two new bacterial DNA primase inhibitors from the plant Polygonum cuspidatumBioorganic & Medicinal Chemistry Letters, 2004
- Protein–protein interfaces: mimics and inhibitorsCurrent Opinion in Chemical Biology, 2001
- A TOPRIM domain in the crystal structure of the catalytic core of Escherichia coli primase confirms a structural link to DNA topoisomerases 1 1Edited by P. E. WrightJournal of Molecular Biology, 2000
- Structure of the zinc-binding domain of Bacillus stearothermophilus DNA primaseStructure, 2000
- The HexamericE. coliDnaB Helicase can Exist in Different Quarternary StatesJournal of Molecular Biology, 1996
- Structure and function of Escherichia coli DnaB protein: Role of the N-terminal domain in helicase activityBiochemistry, 1994
- Organization and evolution of bacterial and bacteriophage primase-helicase systemsJournal of Molecular Evolution, 1992