Cryoelectron Microscopy Reconstructions of the Pseudomonas aeruginosa and Neisseria gonorrhoeae Type IV Pili at Sub-nanometer Resolution.
Cryoelectron Microscopy Reconstructions of the Pseudomonas aeruginosa and Neisseria gonorrhoeae Type IV Pili at Sub-nanometer Resolution.
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亚纳米分辨率下铜绿假单胞菌和 IV 型菌毛淋病奈瑟菌的冷冻电子显微镜重建。
DOI：
10.1016/j.str.2017.07.016
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发表时间：
2017
期刊：
影响因子：
--
通讯作者：
Craig,Lisa
中科院分区：
文献类型：
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作者：
Wang,Fengbin;Coureuil,Mathieu;Osinski,Tomasz;Orlova,Albina;Altindal,Tuba;Gesbert,Gaël;Nassif,Xavier;Egelman,EdwardH;Craig,Lisa
我们在这里报告了两种重要人类病原体——铜绿假单胞菌和淋病奈瑟菌——的 IV 型菌毛 (T4P) 的冷冻电镜重建，分辨率分别为 ∼ 8 和 5 Å。这两种结构揭示了菌毛表面上菌毛球状结构域的不同排列，这赋予了不同的螺旋参数，但在丝核中保守的 N 端 α 螺旋 α1 的堆积相似。与 P 的 X 射线晶体结构中看到的连续 α 螺旋相反。 铜绿假单胞菌和N. 淋球菌毛菌素亚基，菌毛细丝中的 α1 有一个熔化的片段，位于保守的螺旋断裂残基 Gly14 和 Pro22 之间，如脑膜炎奈瑟菌 T4P 中所见。通过诱变，我们发现 Pro22 对于菌毛组装至关重要，Thr2 和 Glu5 也是如此，它们位于疏水丝核心中相互作用。这些结构为理解 T4P 组装、功能和生物物理特性提供了框架。
We report here cryoelectron microscopy reconstructions of type IV pili (T4P) from two important human pathogens,Pseudomonas aeruginosaandNeisseria gonorrhoeae, at ∼ 8 and 5 Å resolution, respectively. The two structures reveal distinct arrangements of the pilin globular domains on the pilus surfaces, which impart different helical parameters, but similar packing of the conserved N-terminal α helices, α1, in the filament core. In contrast to the continuous α helix seen in the X-ray crystal structures of theP. aeruginosaandN. gonorrhoeaepilin subunits, α1 in the pilus filaments has a melted segment located between conserved helix-breaking residues Gly14 and Pro22, as seen for theNeisseria meningitidisT4P. Using mutagenesis we show that Pro22 is critical for pilus assembly, as are Thr2 and Glu5, which are positioned to interact in the hydrophobic filament core. These structures provide a framework for understanding T4P assembly, function, and biophysical properties.