The Cryoelectron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod.

The Cryoelectron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod.
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DOI:
10.1016/j.str.2017.10.004
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发表时间:
2017-12-05
期刊:
Structure (London, England : 1993)
影响因子:
--
通讯作者:
Waksman G
Waksman G
中科院分区:
其他
文献类型:
--
作者:
Hospenthal MK;Zyla D;Costa TRD;Redzej A;Giese C;Lillington J;Glockshuber R;Waksman G

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粘附分子伴侣-引导皮利是一种长的超分子蛋白质纤维,存在于许多病原菌的表面。尿路致病性大肠杆菌(UPEC)的1型和P皮利在尿路定植过程中起重要作用,分别介导与膀胱和肾脏的附着。螺旋菌毛杆的生物力学特性使它们能够响应于流动诱导的力而可逆地解旋,从而使UPEC能够在尿路的独特和恶劣环境中保持立足点。在这里,我们提供了4.2- 100分辨率cryo-EM结构的1型菌毛杆,这与以前的P菌毛杆结构合理化显着的“弹簧般”的性能的伴侣-引座皮利。1型毛杆的冷冻EM结构在螺旋参数方面与之前通过混合方法确定的结构不同。我们提供的证据表明,这些结构差异源于不同的四级结构的皮利组装在体内和体外。1型伴侣蛋白-usher菌毛杆的原子结构通过冷冻-EM解析。与P菌毛杆结构的比较揭示了相似性和关键差异。我们天然纯化的FimA杆结构不同于体外组装的杆结构。大肠杆菌介导宿主识别和粘附。Hospenthal等人提出了1型菌毛杆的冷冻电镜结构,解释了其“弹簧样”的生物力学特性。生化数据表明,杆可以存在于一个以上的螺旋四级大会。
Adhesive chaperone-usher pili are long, supramolecular protein fibers displayed on the surface of many bacterial pathogens. The type 1 and P pili of uropathogenic Escherichia coli (UPEC) play important roles during urinary tract colonization, mediating attachment to the bladder and kidney, respectively. The biomechanical properties of the helical pilus rods allow them to reversibly uncoil in response to flow-induced forces, allowing UPEC to retain a foothold in the unique and hostile environment of the urinary tract. Here we provide the 4.2-Å resolution cryo-EM structure of the type 1 pilus rod, which together with the previous P pilus rod structure rationalizes the remarkable “spring-like” properties of chaperone-usher pili. The cryo-EM structure of the type 1 pilus rod differs in its helical parameters from the structure determined previously by a hybrid approach. We provide evidence that these structural differences originate from different quaternary structures of pili assembled in vivo and in vitro. The atomic structure of the type 1 chaperone-usher pilus rod was solved by cryo-EM A comparison to the P pilus rod structure reveals similarities and key differences Our natively purified FimA rod structure differs to an in vitro assembled rod structure Unfolding kinetics suggest different quaternary assemblies are possible for FimA rods Chaperone-usher pili are crucial virulence factors of uropathogenic E. coli that mediate host recognition and adhesion. Hospenthal et al. present the cryo-EM structure of the type 1 pilus rod explaining its “spring-like” biomechanical properties. Biochemical data suggest that the rod can exist in more than one helical quaternary assembly.
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