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Streptomyces are filamentous bacteria with a complex developmental life cycle characterized by the formation of spore-forming aerial hyphae. Transcription of the chaplin and rodlin genes, which are essential for aerial hyphae production, is directed by the extracytoplasmic function (ECF) factor BldN, which is in turn controlled by an antifactor, RsbN. RsbN shows no sequence similarity to known antifactors and binds and inhibits BldN in an unknown manner. Here we describe the 2.23 Å structure of the RsbN–BldN complex. The structure shows that BldN harbors 2 and 4 domains that are individually similar to other ECF domains, which bind −10 and −35 promoter regions, respectively. The antiRsbN consists of three helices, with 3 forming a long helix embraced between BldN 2 and 4 while RsbN 1– 2 dock against 4 in a manner that would block −35 DNA binding. RsbN binding also freezes BldN in a conformation inactive for simultaneous −10 and −35 promoter interaction and RNAP binding. Strikingly, RsbN is structurally distinct from previously solved antiproteins. Thus, these data characterize the molecular determinants controlling a central Streptomyces developmental switch and reveal RsbN to be the founding member of a new structural class of

The crystal structure of the RsbN–σBldN complex from Streptomyces venezuelae defines a new structural class of anti-σ factor