Type IV pilin structure and assembly:: X-ray and EM analyses of Vibrio cholerae toxin-coregulated pilus and Pseudomonas aeruginosa PAK pilin
Type IV pilin structure and assembly:: X-ray and EM analyses of Vibrio cholerae toxin-coregulated pilus and Pseudomonas aeruginosa PAK pilin
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DOI：
10.1016/s1097-2765(03)00170-9
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发表时间：
2003-05-01
期刊：
影响因子：
16
通讯作者：
Tainer, JA
中科院分区：
文献类型：
--
作者：
Craig, L;Taylor, RK;Tainer, JA
菌毛蛋白组装成IV型皮利是引起霍乱、肺炎、淋病和脑膜炎等疾病的细菌病原体的毒力所必需的。可溶性，N-末端截短菌毛从霍乱弧菌毒素共调节菌毛（TCP）和全长PAK菌毛从铜绿假单胞菌的晶体结构揭示了一种新的TCP折叠，但IV型菌毛的共享架构。在每个菌毛蛋白亚基中，保守的、延伸的、N-末端α螺旋被β链包裹，锚定结构可变的球状头部。在组装的菌毛内部，其特征在于通过冷冻电子显微镜和晶体学，扩展的疏水性α螺旋使多亚基接触以提供机械强度和柔性。在外部，适应性头部的不同相互作用有助于抗原性、运动性、粘附性和集落形成中菌毛功能特异性的表面变化。
Pilin assembly into type IV pili is required for virulence by bacterial pathogens that cause diseases such as cholera, pneumonia, gonorrhea, and meningitis. Crystal structures of soluble, N-terminally truncated pilin from Vibrio cholera toxin-coregulated pilus (TCP) and full-length PAK pilin from Pseudomonas aeruginosa reveal a novel TCP fold, yet a shared architecture for the type IV pilins. In each pilin subunit a conserved, extended, N-terminal alpha helix wrapped by beta strands anchors the structurally variable globular head. Inside the assembled pilus, characterized by cryo-electron microscopy and crystallography, the extended hydrophobic alpha helices make multisubunit contacts to provide mechanical strength and flexibility. Outside, distinct interactions of adaptable heads contribute surface variation for specificity of pilus function in antigenicity, motility, adhesion, and colony formation.