6KRY
Structure of staphylococcal enterotoxin SEN
6KRY の概要
エントリーDOI | 10.2210/pdb6kry/pdb |
分子名称 | Enterotoxin SEN variant (2 entities in total) |
機能のキーワード | staphylococcal enterotoxin, sen, allergen |
由来する生物種 | Staphylococcus aureus |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 26145.22 |
構造登録者 | |
主引用文献 | Zeng, C.,Liu, Z.,Han, Z. Structure of Staphylococcal Enterotoxin N: Implications for Binding Properties to Its Cellular Proteins. Int J Mol Sci, 20:-, 2019 Cited by PubMed Abstract: strains produce a unique family of immunostimulatory exotoxins termed as bacterial superantigens (SAgs), which cross-link major histocompatibility complex class II (MHC II) molecule and T-cell receptor (TCR) to stimulate large numbers of T cells at extremely low concentrations. SAgs are associated with food poisoning and toxic shock syndrome. To date, 26 genetically distinct staphylococcal SAgs have been reported. This study reports the first X-ray structure of newly characterized staphylococcal enterotoxin N (SEN). SEN possesses the classical two domain architecture that includes an N-terminal oligonucleotide-binding fold and a C-terminal β-grasp domain. Amino acid and structure alignments revealed that several critical amino acids that are proposed to be responsible for MHC II and TCR molecule engagements are variable in SEN, suggesting that SEN may adopt a different binding mode to its cellular receptors. This work helps better understand the mechanisms of action of SAgs. PubMed: 31775346DOI: 10.3390/ijms20235921 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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