Enterotoxin type B
| Enterotoxin type B | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | entB | ||||||
UniProt | P01552 | ||||||
| |||||||
| Staphylococcal/Streptococcal toxin, N-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| |||||||||
| Staphylococcal/Streptococcal toxin, beta-grasp domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Stap_Strp_tox_C | ||||||||
SCOP2 | 1se3 / SCOPe / SUPFAM | ||||||||
| |||||||||
In the field of
Additionally, this protein is one of the causative agents of toxic shock syndrome.
Function
The function of this protein is to facilitate the infection of the
Structure
All of these toxins share a similar two-domain fold (N and C-terminal domains) with a long alpha-helix in the middle of the molecule, a characteristic beta-barrel known as the "oligosaccharide/oligonucleotide fold" at the N-terminal domain and a beta-grasp motif at the C-terminal domain. Each superantigen possesses slightly different binding mode(s) when it interacts with MHC class II molecules or the T-cell receptor.[4]
N-terminal domain
The
The N-terminal domain contains regions involved in Major Histocompatibility Complex class II association. It is a five stranded beta barrel that forms an OB fold.[6][7][8]
C-terminal domain
The beta-grasp domain has some structural similarities to the beta-grasp motif present in immunoglobulin-binding domains, ubiquitin, 2Fe-2 S ferredoxin and translation initiation factor 3 as identified by the SCOP database.