PDBsum entry 5fk9

Immune system

PDB id: 5fk9

Contents

Protein chains

198 a.a.

241 a.a.

216 a.a.

Waters ×4

PDB id:

5fk9

Name:

Immune system

Title:

Crystal structure of staphylococcal enterotoxin a f47a mutant in complex with a t cell receptor

Structure:

T cell receptor alpha chain. Chain: a. Fragment: immunoglobulin domains, residues 1-206. Engineered: yes. Other_details: variable domain trav22 and constant domain trac1. T cell receptor beta chain. Chain: b. Fragment: immunoglobulin domains, residues 1-243. Engineered: yes.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Cell: t-lymphocyte. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: star. Staphylococcus aureus. Organism_taxid: 1280.

Resolution:

3.10Å R-factor: 0.259 R-free: 0.291

Authors:

K.E.J.Rodstrom,P.Regenthal,K.Lindkvist-Petersson

Key ref:

K.E.Rödström et al. (2016). Two common structural motifs for TCR recognition by staphylococcal enterotoxins. Sci Rep, 6, 25796. PubMed id: 27180909 DOI: 10.1038/srep25796

Date:

15-Oct-15 Release date: 25-May-16

Protein chain

A0A0B4J277  (TVA22_HUMAN) -  T cell receptor alpha variable 22 from Homo sapiens

Seq: 110 a.a.

Struc: 198 a.a.*

Protein chain

P01848  (TCA_HUMAN) -  T cell receptor alpha chain constant from Homo sapiens

Seq: 140 a.a.

Struc: 198 a.a.*

Protein chain

A0A5A3  (A0A5A3_HUMAN) -  V_segment translation product (Fragment) from Homo sapiens

Seq: 116 a.a.

Struc: 241 a.a.*

Protein chain

A0A5B9  (TRBC2_HUMAN) -  T cell receptor beta constant 2 from Homo sapiens

Seq: 178 a.a.

Struc: 241 a.a.*

Protein chain

P0A0L2  (ETXA_STAAU) -  Enterotoxin type A from Staphylococcus aureus

Seq: 257 a.a.

Struc: 216 a.a.

* PDB and UniProt seqs differ at 9 residue positions (black crosses)

DOI no: 10.1038/srep25796

Sci Rep 6:25796 (2016)

PubMed id: 27180909

Two common structural motifs for TCR recognition by staphylococcal enterotoxins.

K.E.Rödström, P.Regenthal, C.Bahl, A.Ford, D.Baker, K.Lindkvist-Petersson.

ABSTRACT

Superantigens are toxins produced by Staphylococcus aureus, called staphylococcal enterotoxins (abbreviated SEA to SEU). They can cross-link the T cell receptor (TCR) and major histocompatibility complex class II, triggering a massive T cell activation and hence disease. Due to high stability and toxicity, superantigens are potential agents of bioterrorism. Hence, antagonists may not only be useful in the treatment of disease but also serve as countermeasures to biological warfare. Of particular interest are inhibitors against SEA and SEB. SEA is the main cause of food poisoning, while SEB is a common toxin manufactured as a biological weapon. Here, we present the crystal structures of SEA in complex with TCR and SEE in complex with the same TCR, complemented with computational alanine-scanning mutagenesis of SEA, SEB, SEC3, SEE, and SEH. We have identified two common areas that contribute to the general TCR binding for these superantigens. This paves the way for design of single antagonists directed towards multiple toxins.