4GIT

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

Summary for 4GIT

• Entry DOI: 10.2210/pdb4git/pdb
• Descriptor: Lon protease, SULFATE ION (3 entities in total)
• Functional Keywords: dna binding, hydrolase
• Biological source: Brevibacillus thermoruber
• Cellular location: Cytoplasm (By similarity): Q84FG5
• Total number of polymer chains: 2
• Total formula weight: 28893.32

Authors

Chen, Y.D.,Chang, Y.Y.,Hsu, C.H. (deposition date: 2012-08-09, release date: 2013-09-11, Last modification date: 2023-11-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.882 Å)