4GIT

Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber

4GIT の概要

• エントリーDOI: 10.2210/pdb4git/pdb
• 分子名称: Lon protease, SULFATE ION (3 entities in total)
• 機能のキーワード: dna binding, hydrolase
• 由来する生物種: Brevibacillus thermoruber
• 細胞内の位置: Cytoplasm (By similarity): Q84FG5
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28893.32

構造登録者

Chen, Y.D.,Chang, Y.Y.,Hsu, C.H. (登録日: 2012-08-09, 公開日: 2013-09-11, 最終更新日: 2023-11-08)

主引用文献

Lee, A.Y.,Chen, Y.D.,Chang, Y.Y.,Lin, Y.C.,Chang, C.F.,Huang, S.J.,Wu, S.H.,Hsu, C.H.
Structural basis for DNA-mediated allosteric regulation facilitated by the AAA(+) module of Lon protease.
Acta Crystallogr.,Sect.D, 70:218-230, 2014

PubMed Abstract: 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 α 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 α 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.

PubMed: 24531457
DOI: 10.1107/S139900471302631X

実験手法

X-RAY DIFFRACTION (2.882 Å)