輸送シャペロンFliTの構造とべん毛形成制御の分子機構

書誌事項

タイトル別名
  • Structure of the Flagellar Type III Export Chaperone FliT, and Its Regulatory Mechanism of Flagellar Assembly
  • ユソウ シャペロン FliT ノ コウゾウ ト ベンモウ ケイセイ セイギョ ノ ブンシ キコウ

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Flagellar export chaperones are multifunctional small proteins required for efficient construction of the bacterial flagellum. FliT is a flagellar export chaperone for the filament-capping protein FliD. We have determined the structure of FliT at 3.2 Å resolution. FliT adopts an anti-parallel α-helical bundle structure with a unique C-terminal helical segment of flexible orientation. The structure and following genetic and biochemical studies indicated that a conformational change of the C-terminal segment is responsible for switching the binding partners to regulate gene expression and protein export. This finding reveals how the complex pattern of interactions with various binding partners is regulated by a conformational change of such a small protein molecule.

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