In:
Acta Crystallographica Section D Biological Crystallography, International Union of Crystallography (IUCr), Vol. 70, No. 2 ( 2014-02-01), p. 218-230
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.
Type of Medium:
Online Resource
ISSN:
1399-0047
DOI:
10.1107/S139900471302631X
DOI:
10.1107/S139900471302631X/yt5057sup1.pdf
Language:
Unknown
Publisher:
International Union of Crystallography (IUCr)
Publication Date:
2014
detail.hit.zdb_id:
2020492-9
detail.hit.zdb_id:
2968623-4
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