NMR assignments for the telokin-like domain of bacteriophage P22 coat protein.
NMR assignments for the telokin-like domain of bacteriophage P22 coat protein.
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DOI：
10.1007/s12104-012-9422-x
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发表时间：
2013-10
影响因子：
0.9
通讯作者：
Alexandrescu AT
中科院分区：
文献类型：
--
作者：
Rizzo AA;Fraser LC;Sheftic SR;Suhanovsky MM;Teschke CM;Alexandrescu AT
噬菌体 P22 病毒体由相同的外壳蛋白单体通过复杂的反应组装而成，该反应通常在有尾双链 DNA 噬菌体和病毒中保守。双链 DNA 病毒的许多外壳蛋白具有基于 HK97 折叠的结构，但在某些病毒和噬菌体中还有其他结构域。最近在 P22 外壳蛋白中发现了一个“telokin 样”结构域，但其结构尚未以高分辨率表征。最近发表的两个低分辨率冷冻电镜重建结果表明，telokin 样结构域的折叠明显不同，这导致了关于其在衣壳组装和稳定性中的功能的不同结论。在这里，我们报告了 telokin 样结构域的 1H、15N 和 13C NMR 共振归属。根据本研究中获得的化学位移值预测的二级结构与两个冷冻电镜模型存在显着差异，但与其中一个模型更加一致。特别是，一种模型中功能重要的“D-环”显示出化学位移和溶剂交换保护与 β-折叠结构更加一致。我们的工作将为 telokin 样结构域的高分辨率 NMR 结构测定奠定基础，这将有助于改进冷冻电镜模型，进而更好地了解外壳蛋白单体如何组装成毒力所需的二十面体衣壳。
The bacteriophage P22 virion is assembled from identical coat protein monomers in a complex reaction that is generally conserved among tailed, double-stranded DNA bacteriophages and viruses. Many coat proteins of dsDNA viruses have structures based on the HK97 fold, but in some viruses and phages there are additional domains. In the P22 coat protein a “telokin-like” domain was recently identified, whose structure has not yet been characterized at high-resolution. Two recently published low-resolution cryo-EM reconstructions suggest markedly different folds for the telokin-like domain, that lead to alternative conclusions about its function in capsid assembly and stability. Here we report 1H, 15N, and 13C NMR resonance assignments for the telokin-like domain. The secondary structure predicted from the chemical shift values obtained in this work shows significant discrepancies from both cryo-EM models but agrees better with one of the models. In particular, the functionally important “D-loop” in one model shows chemical shifts and solvent exchange protection more consistent with β-sheet structure. Our work will set the basis for a high-resolution NMR structure determination of the telokin-like domain that will help improve the cryo-EM models, and in turn lead to a better understanding of how coat protein monomers assemble into the icosahedral capsids required for virulence.
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影响因子：
14.9
作者：
Cole C;Barber JD;Barton GJ
通讯作者：
Barton GJ
影响因子：
6.8
作者：
Johnson JE
通讯作者：
Johnson JE
影响因子：
2.9
作者：
Vranken, WF;Boucher, W;Laue, ED
通讯作者：
Laue, ED
DOI：
10.1073/pnas.1015739108
发表时间：
2011-01-25
影响因子：
11.1
作者：
Chen, Dong-Hua;Baker, Matthew L.;Chiu, Wah
通讯作者：
Chiu, Wah
影响因子：
3.7
作者：
Suhanovsky, Margaret M.;Teschke, Carolyn M.
通讯作者：
Teschke, Carolyn M.