Crystal structure of the N-terminal domain of Geobacillus kaustophilus HTA426 DnaD protein

Cheng-Yang Huang; Yi-Wei Chang; Wei-Ti Chen

doi:10.1016/j.bbrc.2008.07.160

Crystal structure of the N-terminal domain of Geobacillus kaustophilus HTA426 DnaD protein

Biochem Biophys Res Commun. 2008 Oct 17;375(2):220-4. doi: 10.1016/j.bbrc.2008.07.160. Epub 2008 Aug 12.

Authors

Cheng-Yang Huang¹, Yi-Wei Chang, Wei-Ti Chen

Affiliation

¹ Department of Biomedical Sciences, Chung Shan Medical University, No. 110, Sec. 1, Chien-Kuo N. Road, Taichung 402, Taiwan. cyhuang@csmu.edu.tw

PMID: 18703019
DOI: 10.1016/j.bbrc.2008.07.160

Abstract

The DnaD is one of the primosomal proteins that are required for initiation and re-initiation of chromosomal DNA replication in Gram-positive bacteria. The DnaD protein is composed of two major structural domains: an N-terminal oligomerization domain and a C-terminal ssDNA binding domain. Here, we report the crystal structure of the N-terminal domain (aa 1-128) of DnaD (DnaDn) of Geobacillus kaustophilus HTA426 at 2.3A resolution. The structure of DnaDn reveals an extended winged-helix fold, a typical double-stranded DNA binding motif as winged-helix proteins. DnaDn formed tetramers in the crystalline state, but the results of gel filtration chromatography further indicated that this domain of DnaD was a stable dimer in solution. The structural analysis of DnaDn may suggest the binding sites for DNA and DnaB, and an assembly mechanism for Gram-positive bacterial DNA replication primosome.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacillaceae / metabolism*
Bacterial Proteins / chemistry*
Binding Sites
Crystallography, X-Ray
DNA-Binding Proteins / chemistry*
Dimerization
Models, Molecular
Protein Structure, Tertiary

Substances

Bacterial Proteins
DNA-Binding Proteins