Summary for 6DXO
| Entry DOI | 10.2210/pdb6dxo/pdb |
| Descriptor | RNA polymerase ECF-subfamily sigma factor, BldN (3 entities in total) |
| Functional Keywords | bldn, rsbn, sigma, anti-sigma, ecf, transcription |
| Biological source | Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745) More |
| Total number of polymer chains | 2 |
| Total formula weight | 26612.06 |
| Authors | Schumacher, M.A. (deposition date: 2018-06-29, release date: 2018-07-11, Last modification date: 2023-10-11) |
| Primary citation | Schumacher, M.A.,Bush, M.J.,Bibb, M.J.,Ramos-Leon, F.,Chandra, G.,Zeng, W.,Buttner, M.J. The crystal structure of the RsbN-sigma BldN complex from Streptomyces venezuelae defines a new structural class of anti-sigma factor. Nucleic Acids Res., 46:7405-7417, 2018 Cited by PubMed Abstract: 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) σ factor BldN, which is in turn controlled by an anti-σ factor, RsbN. RsbN shows no sequence similarity to known anti-σ factors 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 σ2 and σ4 domains that are individually similar to other ECF σ domains, which bind -10 and -35 promoter regions, respectively. The anti-σ RsbN consists of three helices, with α3 forming a long helix embraced between BldN σ2 and σ4 while RsbN α1-α2 dock against σ4 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 anti-σ proteins. 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 anti-σ factor. PubMed: 29905823DOI: 10.1093/nar/gky493 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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