| Literature DB >> 23771856 |
Yu-Da Chen1, Shih-Hsiung Wu, Chun-Hua Hsu.
Abstract
Lon is an ATPases associated with diverse cellular activities protease and belongs to a unique group that binds DNA. The α sub-domain of Lon protease is responsible for DNA-binding, but the structural information for its DNA-recognition mode is still limited. Here, we report (1)H, (15)N and (13)C backbone assignment for the α sub-domain from Brevibacillus thermoruber Lon protease as the basis for the elucidation of its structure and interactions with DNA, necessary for understanding the allosteric regulatory mechanism of the enzymatic function.Entities:
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Year: 2013 PMID: 23771856 DOI: 10.1007/s12104-013-9490-6
Source DB: PubMed Journal: Biomol NMR Assign ISSN: 1874-270X Impact factor: 0.746