Crystallization and X-ray diffraction analysis of the DNA-remodelling protein DnaD from Bacillus subtilis
- School of Pharmacy and Centre for Biomolecular Sciences, University of Nottingham (United Kingdom)
- School of Chemistry and Centre for Biomolecular Sciences, University of Nottingham (United Kingdom)
Crystallization and preliminary X-ray diffraction analysis of the two domains of DnaD from B. subtilis is reported. The DnaD protein is an essential component of the chromosome-replication machinery of the Gram-positive bacterium Bacillus subtilis and is part of the primosomal cascade that ultimately loads the replicative ring helicase DnaC onto DNA. Moreover, DnaD is a global regulator of DNA architecture, as it forms higher order nucleoprotein structures in order to open supercoiled DNA. Here, the crystallization and preliminary X-ray diffraction analysis of the two domains of DnaD from B. subtilis are reported. Crystals of the N-terminal domain are trigonal, with either P3{sub 1}21 or P3{sub 2}21 space-group symmetry, and diffracted X-rays to 2.0 Å resolution; crystals of the C-terminal domain are hexagonal, with space group P6{sub 1} or P6{sub 5}, and diffracted X-rays to 2.9 Å resolution in-house. Determination of the structure of the DnaD domains will provide insight into how remodelling of the nucleoid is associated with priming of replication in the model Gram-positive organism B. subtilis.
- OSTI ID:
- 22360266
- Journal Information:
- Acta Crystallographica. Section F, Vol. 63, Issue Pt 2; Other Information: PMCID: PMC2330131; PMID: 17277452; PUBLISHER-ID: hc5023; OAI: oai:pubmedcentral.nih.gov:2330131; Copyright (c) International Union of Crystallography 2007; This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html.; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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