2VN2

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

Summary for 2VN2

• Entry DOI: 10.2210/pdb2vn2/pdb
• Descriptor: CHROMOSOME REPLICATION INITIATION PROTEIN, MAGNESIUM ION (3 entities in total)
• Functional Keywords: dnad, dna replication, primosome, replication
• Biological source: GEOBACILLUS KAUSTOPHILUS HTA426
• Total number of polymer chains: 4
• Total formula weight: 58640.44

Authors

Huang, C.-Y.,Chang, Y.-W.,Chen, W.-T.,Sun, Y.-J.,Hsiao, C.-D. (deposition date: 2008-01-30, release date: 2008-08-12, Last modification date: 2024-05-08)

Primary citation

Huang, C.-Y.,Chang, Y.-W.,Chen, W.-T.
Crystal Structure of the N-Terminal Domain of Geobacillus Kaustophilus Hta426 Dnad Protein.
Biochem.Biophys.Res.Commun., 375:220-, 2008

PubMed 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.

PubMed: 18703019
DOI: 10.1016/J.BBRC.2008.07.160

Experimental method

X-RAY DIFFRACTION (2.3 Å)