Backbone resonance assignments of the α sub-domain of Brevibacillus thermoruber Lon protease
Journal
Biomolecular NMR Assignments
Journal Volume
8
Journal Volume
8
Journal Issue
2
Journal Issue
2
Pages
233-236
Start Page
233
End Page
236
ISSN
18742718
Date Issued
2013-06-15
Author(s)
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.
Subjects
AAA+ protein family
DNA binding
Lon protease
NMR
α Sub-domain
Publisher
Kluwer Academic Publishers
Type
journal article