Article
The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity.
The Journal of biological chemistry - 20 Oct 2006
Merz Frieder, Hoffmann Anja, Rutkowska Anna, Zachmann-Brand Beate, Bukau Bernd, Deuerling Elke
Abstract excerpt
In bacteria, ribosome-bound Trigger Factor assists the folding of newly synthesized proteins. The N-terminal domain (N) of Trigger Factor mediates ribosome binding, whereas the middle domain (P) harbors peptidyl-prolyl isomerase activity. The function of the C-terminal domain (C) has remained enigmatic due to structural instability in isolation. Here, we have characterized a stabilized version of the C domain...
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