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| ==1.8 A structure of RsbN-BldN complex.== | | ==1.8 A structure of RsbN-BldN complex.== |
- | <StructureSection load='6dxo' size='340' side='right' caption='[[6dxo]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='6dxo' size='340' side='right'caption='[[6dxo]], [[Resolution|resolution]] 1.80Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6dxo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Strvp Strvp]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6c03 6c03]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DXO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DXO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6dxo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_venezuelae_ATCC_10712 Streptomyces venezuelae ATCC 10712]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6c03 6c03]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DXO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DXO FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SVEN_3185 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=953739 STRVP]), SVEN_3186 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=953739 STRVP])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6dxo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dxo OCA], [http://pdbe.org/6dxo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dxo RCSB], [http://www.ebi.ac.uk/pdbsum/6dxo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dxo ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6dxo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dxo OCA], [https://pdbe.org/6dxo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dxo RCSB], [https://www.ebi.ac.uk/pdbsum/6dxo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dxo ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/F2R911_STRVP F2R911_STRVP] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| </div> | | </div> |
| <div class="pdbe-citations 6dxo" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6dxo" style="background-color:#fffaf0;"></div> |
| + | |
| + | ==See Also== |
| + | *[[Ectonucleotide pyrophosphatase/phosphodiesterase 3D structures|Ectonucleotide pyrophosphatase/phosphodiesterase 3D structures]] |
| + | *[[Sigma factor 3D structures|Sigma factor 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Strvp]] | + | [[Category: Large Structures]] |
- | [[Category: Schumacher, M A]] | + | [[Category: Streptomyces venezuelae ATCC 10712]] |
- | [[Category: Anti-sigma]] | + | [[Category: Schumacher MA]] |
- | [[Category: Bldn]]
| + | |
- | [[Category: Ecf]]
| + | |
- | [[Category: Rsbn]]
| + | |
- | [[Category: Sigma]]
| + | |
- | [[Category: Transcription]]
| + | |
| Structural highlights
Function
F2R911_STRVP
Publication Abstract from PubMed
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) sigma factor BldN, which is in turn controlled by an anti-sigma factor, RsbN. RsbN shows no sequence similarity to known anti-sigma factors and binds and inhibits BldN in an unknown manner. Here we describe the 2.23 A structure of the RsbN-BldN complex. The structure shows that BldN harbors sigma2 and sigma4 domains that are individually similar to other ECF sigma domains, which bind -10 and -35 promoter regions, respectively. The anti-sigma RsbN consists of three helices, with alpha3 forming a long helix embraced between BldN sigma2 and sigma4 while RsbN alpha1-alpha2 dock against sigma4 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-sigma 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-sigma factor.
The crystal structure of the RsbN-sigmaBldN complex from Streptomyces venezuelae defines a new structural class of anti-sigma factor.,Schumacher MA, Bush MJ, Bibb MJ, Ramos-Leon F, Chandra G, Zeng W, Buttner MJ Nucleic Acids Res. 2018 Jun 14. pii: 5037724. doi: 10.1093/nar/gky493. PMID:29905823[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schumacher MA, Bush MJ, Bibb MJ, Ramos-Leon F, Chandra G, Zeng W, Buttner MJ. The crystal structure of the RsbN-sigmaBldN complex from Streptomyces venezuelae defines a new structural class of anti-sigma factor. Nucleic Acids Res. 2018 Jun 14. pii: 5037724. doi: 10.1093/nar/gky493. PMID:29905823 doi:http://dx.doi.org/10.1093/nar/gky493
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