Crystallization and preliminary crystallographic characterization of the origin-binding domain of the bacteriophage λ O replication initiator
- Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218 (United States)
- Department of Biophysics and Biophysical Chemistry, Johns Hopkins School of Medicine, Baltimore, MD 21205 (United States)
Crystallization and preliminary diffraction data of the N-terminal 19–139 fragment of the origin-binding domain of bacteriophage λ O replication initiator are reported. The bacteriophage λ O protein binds to the λ replication origin (oriλ) and serves as the primary replication initiator for the viral genome. The binding energy derived from the binding of O to oriλ is thought to help drive DNA opening to facilitate initiation of DNA replication. Detailed understanding of this process is severely limited by the lack of high-resolution structures of O protein or of any lambdoid phage-encoded paralogs either with or without DNA. The production of crystals of the origin-binding domain of λ O that diffract to 2.5 Å is reported. Anomalous dispersion methods will be used to solve this structure.
- OSTI ID:
- 22360338
- Journal Information:
- Acta Crystallographica. Section F, Vol. 63, Issue Pt 6; Other Information: PMCID: PMC2335069; PMID: 17554183; PUBLISHER-ID: bo5019; OAI: oai:pubmedcentral.nih.gov:2335069; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
Similar Records
Structures of minute virus of mice replication initiator protein N-terminal domain: Insights into DNA nicking and origin binding
The crystal structure of bacteriophage λ RexA provides novel insights into the DNA binding properties of Rex-like phage exclusion proteins