2VN2: Crystal Structure Of The N-Terminal Domain Of Dnad Protein From Geobacillus Kaustophilus Hta426

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.
PDB ID: 2VN2Download
MMDB ID: 65974
PDB Deposition Date: 2008/1/30
Updated in MMDB: 2012/08
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Source Organism:
Similar Structures:
Biological Unit for 2VN2: tetrameric; determined by author and by software (PISA)
Molecular Components in 2VN2
Label Count Molecule
Proteins (4 molecules)
Chromosome Replication Initiation Protein
Molecule annotation
Chemicals (4 molecules)
* Click molecule labels to explore molecular sequence information.

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