Cryo-EM structure of a thermostable bacterial nanocompartment.
Cryo-EM structure of a thermostable bacterial nanocompartment.
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DOI：
10.1107/s2052252521001949
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发表时间：
2021-05-01
期刊：
影响因子：
3.9
通讯作者：
Toor N
中科院分区：
文献类型：
--
作者：
Wiryaman T;Toor N
报道了一种耐热细菌纳米隔室的2.0 ä分辨率低温EM结构，该高分辨率结构允许可视化关键细节和新提出的生物功能。蛋白质纳米隔间在细菌和古菌中广泛存在，但其功能尚未被很好地了解。在这里，报告了来自嗜热细菌Thermotoga maritima的纳米隔间的低温EM结构，分辨率为2.0 ä。这种结构的高分辨率表明，E-loop区域中的相互作用对于纳米隔室组装的热稳定性可能是重要的。此外，还对五重轴、三重轴和二聚体界面上的通道进行了评估，以了解它们运输铁的能力。最后，在外壳的外部发现了一个意想不到的黄素配体，表明这个纳米隔间也可能在铁代谢中发挥直接作用。
A 2.0 Å resolution cryo-EM structure of a thermostable bacterial nanocompartment is reported, with the high-resolution structure allowing the visualization of key details and new proposed biological functions. Protein nanocompartments are widespread in bacteria and archaea, but their functions are not yet well understood. Here, the cryo-EM structure of a nanocompartment from the thermophilic bacterium Thermotoga maritima is reported at 2.0 Å resolution. The high resolution of this structure shows that interactions in the E-loop domain may be important for the thermostability of the nanocompartment assembly. Also, the channels at the fivefold axis, threefold axis and dimer interface are assessed for their ability to transport iron. Finally, an unexpected flavin ligand was identified on the exterior of the shell, indicating that this nanocompartment may also play a direct role in iron metabolism.