Structure of a protein-DNA complex essential for DNA protection in spores of Bacillus species
Structure of a protein-DNA complex essential for DNA protection in spores of Bacillus species
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DOI：
10.1073/pnas.0708244105
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发表时间：
2008-02-26
影响因子：
11.1
通讯作者：
Jedrzejas, Mark J.
中科院分区：
文献类型：
--
作者：
Lee, Ki Seog;Bumbaca, Daniela;Jedrzejas, Mark J.
结合DNA的α/β型小分子酸溶蛋白(SASPs)通过保护芽胞DNA免受干燥、高温、有毒化学物质、酶和紫外线辐射的破坏，是芽孢杆菌芽胞抗性和长期存活的主要因素。现在，我们报道了与10-bp DNA双链结合的α/β型SASP在2.1埃分辨率下的晶体结构。在该复合体中，α/β型SASP采用螺旋-转角-螺旋基序，通过细沟接触与DNA相互作用，以二聚体的形式与DNA结合约6bP，DNA呈A-B型构象。该复合体的结构为了解DNA和α/β型SASP保护的分子细节提供了重要的见解。
The DNA-binding alpha/beta-type small acid-soluble proteins (SASPs) are a major factor in the resistance and long-term survival of spores of Bacillus species by protecting spore DNA against damage due to desiccation, heat, toxic chemicals, enzymes, and UV radiation. We now report the crystal structure at 2.1 angstrom resolution of an alpha/beta-type SASP bound to a 10-bp DNA duplex. In the complex, the alpha/beta-type SASP adopt a helix-turn- helix motif, interact with DNA through minor groove contacts, bind to approximate to 6 bp of DNA as a dimer, and the DNA is in an A-B type conformation. The structure of the complex provides important insights into the molecular details of both DNA and alpha/beta-type SASP protection in the complex and thus also in spores.