Crystallographic insights into the autocatalytic assembly mechanism of a bacteriophage tail spike.
Crystallographic insights into the autocatalytic assembly mechanism of a bacteriophage tail spike.
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DOI：
10.1016/j.molcel.2009.04.009
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发表时间：
2009-05-15
期刊：
影响因子：
16
通讯作者：
Rossmann, Michael G.
中科院分区：
文献类型：
--
作者：
Xiang, Ye;Leiman, Petr G.;Li, Long;Grimes, Shelley;Anderson, Dwight L.;Rossmann, Michael G.
尾部噬菌体φ29有12个“附件”（基因产物12，gp12）附着在其颈部区域，参与宿主细胞识别和进入。在细胞中，gp12单体在组装成三聚体的过程中进行蛋白水解，释放c端结构域。我们在这里报告了蛋白在催化处理前后的晶体结构，并表明gp12的c端结构域是一个“自动伴侣”，有助于三聚化。我们还表明，c端结构域的自动切割是一个后三聚化事件，随后是一个独特的atp依赖性释放。翻译后修饰的n端部分有三个结构域，分别用于将附属物附着到噬菌体上、消化细胞壁壁壁酸和与宿主不可逆结合。结构和序列比较表明，某些真核病毒和细菌病毒以及细菌粘附素可能具有类似于φ29 gp12对枯草芽孢杆菌的成熟机制。
The tailed bacteriophage φ29 has 12 “appendages” (gene product 12, gp12) attached to its neck region that participate in host cell recognition and entry. In the cell, monomeric gp12 undergoes proteolytic processing that releases the C-terminal domain during assembly into trimers. We report here crystal structures of the protein before and after catalytic processing and show that the C-terminal domain of gp12 is an “auto-chaperone” that aids trimerization. We also show that auto-cleavage of the C-terminal domain is a post-trimerization event that is followed by a unique ATP-dependent release. The post-translationally modified N-terminal part has three domains that function to attach the appendages to the phage, digest the cell wall teichoic acids and bind irreversibly to the host, respectively. Structural and sequence comparisons suggest that some eukaryotic and bacterial viruses as well as bacterial adhesins might have similar maturation mechanism as is performed by φ29 gp12 for Bacillus subtilis.
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