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The structure of a disulfide bond can be described by its χ ss dihedral angle between the C β −S γ −S γ −C β atoms, which is usually close to ±90°. The disulfide bond stabilizes the folded form of a protein in several ways: It holds two portions of the protein together, biasing the protein towards the folded topology.
DsbA is a bacterial thiol disulfide oxidoreductase (TDOR). DsbA is a key component of the Dsb (disulfide bond) family of enzymes. DsbA catalyzes intrachain disulfide bond formation as peptides emerge into the cell's periplasm. [2] Structurally, DsbA contains a thioredoxin domain with an inserted helical domain of unknown function. [3]
The C(S)−N bond is short (1.33 Å), indicative of multiple bonding. The dihedral angle between the two dithiocarbamate subunits approaches 90°. [3] Structure of tetramethylthiuram disulfide, emphasizing the 90º dihedral angle between the two planar subunits. Thiuram disulfides are weak oxidants. They can be reduced to dithiocarbamates.
The Disulfide bond oxidoreductase D (DsbD) family is a member of the Lysine Exporter (LysE) Superfamily. [1] A representative list of proteins belonging to the DsbD family can be found in the Transporter Classification Base .
Protein disulfide-isomerase has two catalytic thioredoxin-like domains (active sites), each containing the canonical CGHC motif, and two non catalytic domains. [4] [5] [6] This structure is similar to the structure of enzymes responsible for oxidative folding in the intermembrane space of the mitochondria; an example of this is mitochondrial IMS import and assembly (Mia40), which has 2 ...
The structure of hydrogen disulfide is similar to that of hydrogen peroxide, with C 2 point group symmetry. Both molecules are distinctly nonplanar. The dihedral angle between the H a −S−S and S−S−H b planes is 90.6°, compared with 111.5° in H 2 O 2. The H−S−S bond angle is 92°, close to 90° for unhybridized divalent sulfur. [1]
The formation of multiple native disulfides remains challenging of native peptide synthesis by solid-phase methods. Random chain combination typically results in several products with nonnative disulfide bonds. [41] Stepwise formation of disulfide bonds is typically the preferred method, and performed with thiol protecting groups. [42]
Disulfide bond formation protein B (DsbB) is a protein component of the pathway that leads to disulfide bond formation in periplasmic proteins of Escherichia coli and other bacteria. In Bacillus subtilis it is known as BdbC ( O32217 ).