2OTO

N-terminal fragment of Streptococcus pyogenes M1 protein

2OTO の概要

• エントリーDOI: 10.2210/pdb2oto/pdb
• 分子名称: M protein (1 entity in total)
• 機能のキーワード: helical coiled coil, fibrinogen-binding, virulence factor, surface active protein, toxin
• 由来する生物種: Streptococcus pyogenes serotype M1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 72727.67

構造登録者

McNamara, C.W.,Ghosh, P. (登録日: 2007-02-08, 公開日: 2008-03-18, 最終更新日: 2024-11-20)

主引用文献

McNamara, C.,Zinkernagel, A.S.,Macheboeuf, P.,Cunningham, M.W.,Nizet, V.,Ghosh, P.
Coiled-coil irregularities and instabilities in group A Streptococcus M1 are required for virulence.
Science, 319:1405-1408, 2008

PubMed Abstract: Antigenically variable M proteins are major virulence factors and immunogens of the human pathogen group A Streptococcus (GAS). Here, we report the approximately 3 angstrom resolution structure of a GAS M1 fragment containing the regions responsible for eliciting type-specific, protective immunity and for binding fibrinogen, which promotes M1 proinflammatory and antiphagocytic functions. The structure revealed substantial irregularities and instabilities throughout the coiled coil of the M1 fragment. Similar structural irregularities occur in myosin and tropomyosin, explaining the patterns of cross-reactivity seen in autoimmune sequelae of GAS infection. Sequence idealization of a large segment of the M1 coiled coil enhanced stability but diminished fibrinogen binding, proinflammatory effects, and antibody cross-reactivity, whereas it left protective immunogenicity undiminished. Idealized M proteins appear to have promise as vaccine immunogens.

PubMed: 18323455
DOI: 10.1126/science.1154470

実験手法

X-RAY DIFFRACTION (3.04 Å)