Crystallization and X-ray diffraction analysis of the DNA-remodelling protein DnaD from Bacillus subtilis.
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(1)21 or P3(2)21 space-group symmetry, and diffracted X-rays to 2.0 A resolution; crystals of the C-terminal domain are hexagonal, with space group P6(1) or P6(5), and diffracted X-rays to 2.9 A 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.
Schneider
Sabine
S
School of Pharmacy and Centre for Biomolecular Sciences, University of Nottingham, England.
Carneiro
Maria J V M
MJ
Ioannou
Charikleia
C
Soultanas
Panos
P
Paoli
Max
M
D001412:Bacillus subtilis / Q000737:chemistry* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; C092895:DnaD protein, Bacillus subtilis