Article
Functional analysis of propeptide as an intramolecular chaperone for in vivo folding of subtilisin nattokinase.
FEBS letters - 1 Dec 2010
Jia Yan, Liu Hui, Bao Wei, Weng Meizhi, Chen Wei, Cai Yongjun, Zheng Zhongliang, Zou Guolin
Abstract excerpt
Here, we show that during in vivo folding of the precursor, the propeptide of subtilisin nattokinase functions as an intramolecular chaperone (IMC) that organises the in vivo folding of the subtilisin domain. Two residues belonging to β-strands formed by conserved regions of the IMC are crucial for the folding of the subtilisin domain through direct interactions. An identical protease can fold into different...
Topics
- Amino Acid Sequence
- Bacillus subtilis
- Conserved Sequence
- Kinetics
- Molecular Chaperones
- Molecular Dynamics Simulation
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Protein Folding
- Protein Precursors
- Protein Refolding
- Protein Structure, Secondary