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-Structure paper
タイトル | Structure of a heteropolymeric type 4 pilus from a monoderm bacterium. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 7143, Year 2023 |
掲載日 | 2023年11月6日 |
著者 | Robin Anger / Laetitia Pieulle / Meriam Shahin / Odile Valette / Hugo Le Guenno / Artemis Kosta / Vladimir Pelicic / Rémi Fronzes / |
PubMed 要旨 | 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 ...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 α-helix (α1) - 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 α1 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 Å 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. |
リンク | Nat Commun / PubMed:37932265 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.67 Å |
構造データ | EMDB-17645, PDB-8pfb: |
由来 |
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キーワード | PROTEIN FIBRIL / Bacterial pilus Type 4 pilus |