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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/A0A0B7GU52_STRSA A0A0B7GU52_STRSA] | | [https://www.uniprot.org/uniprot/A0A0B7GU52_STRSA A0A0B7GU52_STRSA] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Type 4 pili (T4P) are important virulence factors, which belong to a superfamily of nanomachines ubiquitous in prokaryotes, called type 4 filaments (T4F). T4F are defined as helical polymers of type 4 pilins. Recent advances in cryo-electron microscopy (cryo-EM) led to structures of several T4F, revealing that the long N-terminal alpha-helix (alpha1) - the trademark of pilins - packs in the centre of the filaments to form a hydrophobic core. In diderm bacteria - all available bacterial T4F structures are from diderm species - a portion of alpha1 is melted (unfolded). Here we report that this architecture is conserved in phylogenetically distant monoderm species by determining the structure of Streptococcus sanguinis T4P. Our 3.7 A resolution cryo-EM structure of S. sanguinis heteropolymeric T4P and the resulting full atomic model including all minor pilins highlight universal features of bacterial T4F and have widespread implications in understanding T4F biology.
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| Structure of a heteropolymeric type 4 pilus from a monoderm bacterium.,Anger R, Pieulle L, Shahin M, Valette O, Le Guenno H, Kosta A, Pelicic V, Fronzes R Nat Commun. 2023 Nov 6;14(1):7143. doi: 10.1038/s41467-023-42872-5. PMID:37932265<ref>PMID:37932265</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 8pfb" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
