The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28.

doi:10.1038/nsb0497-285

Back to search

Article

The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28.

Nature structural biology - 1 Apr 1997

Daughdrill G W, Chadsey M S, Karlinsey J E, Hughes K T, Dahlquist F W

Abstract excerpt

The interaction between the flagellum specific sigma factor, sigma 28, and its inhibitor, FlgM, was examined using multidimensional heteronuclear NMR. Here we observe that free FlgM is mostly unfolded, but about 50% of the residues become structured when bound to sigma 28. Our analysis suggests t...

Topics

Bacterial Proteins
Binding Sites
Flagella
Magnetic Resonance Spectroscopy
Mutation
Protein Binding
Protein Conformation
Protein Folding
Sigma Factor
Time Factors

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.