The N-terminal sequence after residue 247 plays an important role in structure and function of Lon protease from Brevibacillus thermoruber WR-249
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference20 articles.
1. ATP-dependent protease La (Lon) from Escherichia coli;Goldberg;Methods Enzymol.,1994
2. Classification of ATP-dependent proteases Lon and comparison of the active sites of their proteolytic domains;Rotanova;Eur. J. Biochem.,2004
3. Limited proteolysis of E. coli ATP-dependent protease Lon—a unified view of the subunit architecture and characterization of isolated enzyme fragments;Melnikov;Acta Biochim. Pol.,2008
4. Correlation of an adenine-specific conformational change with the ATP-dependent peptidase activity of Escherichia coli Lon;Patterson;Biochemistry,2004
5. Domain structure and ATP-induced conformational changes in Escherichia coli protease Lon revealed by limited proteolysis and autolysis;Vasilyeva;FEBS Lett.,2002
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1. Structure and the Mode of Activity of Lon Proteases from Diverse Organisms;Journal of Molecular Biology;2022-04
2. New insights into structural and functional relationships between LonA proteases and ClpB chaperones;FEBS Open Bio;2019-07-21
3. Involvement of the N-terminal region and its characteristic coiled-coil fragment in the function and structure maintenance of E. coli LonA protease;Russian Journal of Bioorganic Chemistry;2017-07
4. Role of the Inserted α-Helical Domain in E. coli ATP-Dependent Lon Protease Function;Acta Naturae;2017-06-15
5. Functional characterization of LotP from L iberibacter asiaticus;Microbial Biotechnology;2017-04-05
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