最近の研究から
輸送シャペロンFliTの構造とべん毛形成制御の分子機構
2011 年 53 巻 6 号 p. 396-401
詳細
2011 年 53 巻 6 号 p. 396-401
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.
