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Title: Crystallization and X-ray diffraction analysis of the DNA-remodelling protein DnaD from Bacillus subtilis

Abstract

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.

Authors:
 [1]; ; ;  [2];  [1]
  1. School of Pharmacy and Centre for Biomolecular Sciences, University of Nottingham (United Kingdom)
  2. School of Chemistry and Centre for Biomolecular Sciences, University of Nottingham (United Kingdom)
Publication Date:
OSTI Identifier:
22360266
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal 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)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; DNA; PROTEINS; RESOLUTION; RINGS; SPACE GROUPS; SYMMETRY; X-RAY DIFFRACTION

Citation Formats

Schneider, Sabine, Carneiro, Maria J. V. M., Ioannou, Charikleia, Soultanas, Panos, E-mail: panos.soultanas@nottingham.ac.uk, and Paoli, Max, E-mail: panos.soultanas@nottingham.ac.uk. Crystallization and X-ray diffraction analysis of the DNA-remodelling protein DnaD from Bacillus subtilis. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107000474.
Schneider, Sabine, Carneiro, Maria J. V. M., Ioannou, Charikleia, Soultanas, Panos, E-mail: panos.soultanas@nottingham.ac.uk, & Paoli, Max, E-mail: panos.soultanas@nottingham.ac.uk. Crystallization and X-ray diffraction analysis of the DNA-remodelling protein DnaD from Bacillus subtilis. United Kingdom. doi:10.1107/S1744309107000474.
Schneider, Sabine, Carneiro, Maria J. V. M., Ioannou, Charikleia, Soultanas, Panos, E-mail: panos.soultanas@nottingham.ac.uk, and Paoli, Max, E-mail: panos.soultanas@nottingham.ac.uk. Thu . "Crystallization and X-ray diffraction analysis of the DNA-remodelling protein DnaD from Bacillus subtilis". United Kingdom. doi:10.1107/S1744309107000474.
@article{osti_22360266,
title = {Crystallization and X-ray diffraction analysis of the DNA-remodelling protein DnaD from Bacillus subtilis},
author = {Schneider, Sabine and Carneiro, Maria J. V. M. and Ioannou, Charikleia and Soultanas, Panos, E-mail: panos.soultanas@nottingham.ac.uk and Paoli, Max, E-mail: panos.soultanas@nottingham.ac.uk},
abstractNote = {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.},
doi = {10.1107/S1744309107000474},
journal = {Acta Crystallographica. Section F},
number = Pt 2,
volume = 63,
place = {United Kingdom},
year = {Thu Feb 01 00:00:00 EST 2007},
month = {Thu Feb 01 00:00:00 EST 2007}
}
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