Article
Disulphide bond restrains the C-terminal region of thermostable direct hemolysin during folding to promote oligomerization.
The Biochemical journal - 15 Jan 2017
Kundu Nidhi, Tichkule Swapnil, Pandit Shashi Bhushan, Chattopadhyay Kausik
Abstract excerpt
Pore-forming toxins (PFTs) are typically produced as water-soluble monomers, which upon interacting with target cells assemble into transmembrane oligomeric pores. Vibrio parahaemolyticus thermostable direct hemolysin (TDH) is an atypical PFT that exists as a tetramer in solution, prior to membrane binding. The TDH structure highlights a core β-sandwich domain similar to those found in the eukaryotic actinoporin...
Topics
- Amino Acid Sequence
- Bacterial Proteins
- Bacterial Toxins
- Binding Sites
- Cloning, Molecular
- Disulfides
- Erythrocytes
- Escherichia coli
- Gene Expression
- Hemolysin Proteins
- Hemolysis
- Humans
- Kinetics
- Molecular Dynamics Simulation