Open AccessCrystallization and X‐ray diffraction analysis of the DNA‐remodelling protein DnaD from Bacillus subtilis
Author(s) -
Schneider Sabine,
Carneiro Maria J. V. M.,
Ioannou Charikleia,
Soultanas Panos,
Paoli Max
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107000474
Subject(s) - bacillus subtilis , crystallography , dna , helicase , nucleoprotein , biology , chemistry , biophysics , bacteria , biochemistry , genetics , gene , rna
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 P 3 1 21 or P 3 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 P 6 1 or P 6 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 .