Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
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.
Crystal structure of the N-terminal domain of Geobacillus kaustophilus HTA426 DnaD protein.,Huang CY, Chang YW, Chen WT Biochem Biophys Res Commun. 2008 Oct 17;375(2):220-4. Epub 2008 Aug 12. PMID:18703019[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Huang CY, Chang YW, Chen WT. Crystal structure of the N-terminal domain of Geobacillus kaustophilus HTA426 DnaD protein. Biochem Biophys Res Commun. 2008 Oct 17;375(2):220-4. Epub 2008 Aug 12. PMID:18703019 doi:10.1016/j.bbrc.2008.07.160