5DMD

Crystal structure of the flagellar assembly factor FliW

5DMD の概要

• エントリーDOI: 10.2210/pdb5dmd/pdb
• 関連するPDBエントリー: 5DMB
• 分子名称: Flagellar assembly factor FliW (2 entities in total)
• 機能のキーワード: translation, flagellum, assembly factor
• 由来する生物種: Geobacillus thermodenitrificans
• 細胞内の位置: Cytoplasm : A4ISV0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34779.60

構造登録者

Altegoer, F.,Bange, G. (登録日: 2015-09-08, 公開日: 2016-09-07, 最終更新日: 2024-01-17)

主引用文献

Altegoer, F.,Rensing, S.A.,Bange, G.
Structural basis for the CsrA-dependent modulation of translation initiation by an ancient regulatory protein.
Proc.Natl.Acad.Sci.USA, 113:10168-10173, 2016

PubMed Abstract: Regulation of translation is critical for maintaining cellular protein levels, and thus protein homeostasis. The conserved RNA-binding protein CsrA (also called RsmA; for carbon storage regulator and regulator of secondary metabolism, respectively; hereafter called CsrA) represents a well-characterized example of regulation at the level of translation initiation in bacteria. Binding of a CsrA homodimer to the 5'UTR of an mRNA occludes the Shine-Dalgarno sequence, blocking ribosome access for translation. Small noncoding RNAs (sRNAs) can competitively antagonize CsrA activity by a well-understood mechanism. However, the regulation of CsrA by the protein FliW is just emerging. FliW antagonizes the CsrA-dependent repression of translation of the flagellar filament protein, flagellin. Crystal structures of the FliW monomer reveal a novel, minimal β-barrel-like fold. Structural analysis of the CsrA/FliW heterotetramer shows that FliW interacts with a C-terminal extension of CsrA. In contrast to the competitive regulation of CsrA by sRNAs, FliW allosterically antagonizes CsrA in a noncompetitive manner by excluding the 5'UTR from the CsrA-RNA binding site. Our phylogenetic analysis shows that the FliW-mediated regulation of CsrA regulation is the ancestral state in flagellated bacteria. We thus demonstrate fundamental mechanistic differences in the regulation of CsrA by sRNA in comparison with an ancient regulatory protein.

PubMed: 27551070
DOI: 10.1073/pnas.1602425113

実験手法

X-RAY DIFFRACTION (1.45 Å)