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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 that the sigma 28 binding domain of FlgM is contained within the last 57 amino acids of the protein while the first 40...

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PMID: 9095196
DOI: 10.1038/nsb0497-285

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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