title: Backbone resonance assignments of the α sub-domain of Brevibacillus thermoruber Lon protease.
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.
authors.affiliation: Department of Agricultural Chemistry, National Taiwan University, Taipei, 10617, Taiwan.
authors.forename: Yu-Da
authors.initials: YD
authors.lastname: Chen
authors.forename: Shih-Hsiung
authors.initials: SH
authors.lastname: Wu
authors.forename: Chun-Hua
authors.initials: CH
authors.lastname: Hsu
mesh_terms: D000595:Amino Acid Sequence; D058675:Brevibacillus / Q000201:enzymology*; D004247:DNA / Q000378:metabolism; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D049070:Protease La / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary
chemical_list: D004247:DNA; D049070:Protease La