Structure of a heteropolymeric type 4 pilus from a monoderm bacterium

Structure of a heteropolymeric type 4 pilus from a monoderm bacterium
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来自单皮细菌的杂聚型 4 菌毛的结构

DOI:
10.1101/2023.06.15.545089
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发表时间:
2023
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Anger R
Anger R
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4型皮利(T4 P)是重要的毒力因子,属于原核生物中普遍存在的纳米机器超家族,称为4型丝状体(T4 F)。T4 F被定义为4型菌毛蛋白的螺旋聚合物。低温电子显微镜(cryo-EM)的最新进展导致了几种T4 F的结构,揭示了长的N-末端α-螺旋(α1)-菌毛蛋白的商标-包装在细丝的中心形成疏水核心。在双胚层细菌中-所有可用的细菌T4 F结构都来自双胚层物种-α1的一部分被熔化(未折叠)。在这里,我们报告说,这种架构是保守的,在遗传学上遥远的单胚层物种,通过确定的结构ofStreptococcussanguinisT 4P。3.7 μ m分辨率的S.血红蛋白多聚体T4 P和由此产生的包括所有次要菌毛蛋白的全原子模型突出了细菌T4 F的普遍特征,并在理解T4 F生物学方面具有广泛的意义。
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 ofStreptococcus sanguinisT4P. Our 3.7 Å resolution cryo-EM structure ofS. sanguinisheteropolymeric 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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