1POQ

Solution Structure of a Superantigen from Yersinia pseudotuberculosis

1POQ の概要

• エントリーDOI: 10.2210/pdb1poq/pdb
• NMR情報: BMRB: 5836
• 分子名称: YPM (1 entity in total)
• 機能のキーワード: jelly roll fold, immune system
• 由来する生物種: Yersinia pseudotuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13110.63

構造登録者

Donadini, R.,Liew, C.W.,Kwan, A.H.,Mackay, J.P.,Fields, B.A. (登録日: 2003-06-16, 公開日: 2004-01-27, 最終更新日: 2022-03-02)

主引用文献

Donadini, R.,Liew, C.W.,Kwan, A.H.,Mackay, J.P.,Fields, B.A.
Crystal and Solution Structures of a Superantigen from Yersinia pseudotuberculosis Reveal a Jelly-Roll Fold.
Structure, 12:145-156, 2004

PubMed Abstract: Superantigens are a class of microbial proteins with the ability to excessively activate T cells by binding to the T cell receptor. The staphylococcal and streptococcal superantigens are closely related in structure and possess an N-terminal domain that resembles an OB fold and a C-terminal domain similar to a beta-grasp fold. Yersinia pseudotuberculosis produces superantigens, YPMa, YPMb, and YPMc, which have no significant amino acid similarity to other proteins. We have determined the crystal and solution structures of YPMa, which show that the protein has a jelly-roll fold. The closest structural neighbors to YPMa are viral capsid proteins and members of the tumor necrosis factor superfamily. In the crystal structure, YPMa packs as a trimer, another feature shared with viral capsid proteins and TNF superfamily proteins. However, in solution YPMa behaves as a monomer, and any functional relevance of the trimer observed in the crystals is yet to be established.

PubMed: 14725774
DOI: 10.1016/j.str.2003.12.002

実験手法

SOLUTION NMR