期刊
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
卷 70, 期 -, 页码 218-230出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S139900471302631X
关键词
-
资金
- National Science Council [NSC 102-2627-M-400-001, NSC 96-2311-B-001-010, NSC 99-2119-M-002-010]
- National Taiwan University [NTU-ERP-101R8600-1, NTU-ICRP-102R7560-5]
- National Health Research Institutes in Taiwan [102A1-CA-PP-08]
Lon belongs to a unique group of AAA(+) proteases that bind DNA. However, the DNA-mediated regulation of Lon remains elusive. Here, the crystal structure of the alpha subdomain of the Lon protease from Brevibacillus thermoruber (Bt-Lon) is presented, together with biochemical data, and the DNA-binding mode is delineated, showing that Arg518, Arg557 and Arg566 play a crucial role in DNA binding. Electrostatic interactions contributed by arginine residues in the AAA(+) module are suggested to be important to DNA binding and allosteric regulation of enzymatic activities. Intriguingly, Arg557, which directly binds DNA in the alpha subdomain, has a dual role in the negative regulation of ATPase stimulation by DNA and in the domain-domain communication in allosteric regulation of Bt-Lon by substrate. In conclusion, structural and biochemical evidence is provided to show that electrostatic interaction in the AAA(+) module is important for DNA binding by Lon and allosteric regulation of its enzymatic activities by DNA and substrate.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据