Literature DB >> 23771856

Backbone resonance assignments of the α sub-domain of Brevibacillus thermoruber Lon protease.

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.

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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


  1 in total

1.  NMR assignments of the macro domain from Middle East respiratory syndrome coronavirus (MERS-CoV).

Authors:  Yi-Ping Huang; Chao-Cheng Cho; Chi-Fon Chang; Chun-Hua Hsu
Journal:  Biomol NMR Assign       Date:  2016-03-18       Impact factor: 0.746

  1 in total

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