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

被引：13

作者：

Huang, Cheng-Yang ^{[1
]}

Chang, Yi-Wei ^{[2
]}

Chen, Wei-Ti ^{[2
]}

机构：

[1] Chung Shan Med Univ, Dept Biomed Sci, Taichung 402, Taiwan

[2] Natl Tsing Hua Univ, Inst Bioinformat & Struct Biol, Hsinchu, Taiwan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2008年 / 375卷 / 02期

关键词：

primosome; DnaD; PriB; DNA binding; DNA replication;

D O I：

10.1016/j.bbrc.2008.07.160

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The DnaD is one of the primosomal proteins that are required for initiation and re-initiation of chromosornal 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 2.3 angstrom 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. (c) 2008 Elsevier Inc. All rights reserved.

引用

页码：220 / 224

页数：5

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