The Structure of YnaI Implies Structural and Mechanistic Conservation in the MscS Family of Mechanosensitive Channels.
The Structure of YnaI Implies Structural and Mechanistic Conservation in the MscS Family of Mechanosensitive Channels.
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DOI:
10.1016/j.str.2015.06.023
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发表时间:
2015-09-01
期刊:
影响因子:
--
通讯作者:
Rasmussen T
中科院分区:
文献类型:
--
作者:
Böttcher B;Prazak V;Rasmussen A;Black SS;Rasmussen T
Mechanosensitive channels protect bacteria against lysis caused by a sudden drop in osmolarity in their surroundings. Besides the channel of large conductance (MscL) and small conductance (MscS), Escherichia coli has five additional paralogs of MscS that are functional and widespread in the bacterial kingdom. Here, we present the structure of YnaI by cryo-electron microscopy to a resolution of 13 Å. While the cytosolic vestibule is structurally similar to that in MscS, additional density is seen in the transmembrane (TM) region consistent with the presence of two additional TM helices predicted for YnaI. The location of this density suggests that the extra TM helices are tilted, which could induce local membrane curvature extending the tension-sensing paddles seen in MscS. Off-center lipid-accessible cavities are seen that resemble gaps between the sensor paddles in MscS. The conservation of the tapered shape and the cavities in YnaI suggest a mechanism similar to that of MscS. First structure of a large member of the MscS family of mechanosensitive channels The density map indicates extended sensor paddles of tilted transmembrane helices Lipids access the core of YnaI and fill cavities which are similar to gaps in MscS These cavities and the tilted helices could lay the basis for tension sensing Mechanosensitive channels of the MscS family are found in all kingdoms of life and protect bacteria against osmotic shock. Böttcher et al. provide the first structural insights into a larger family member, YnaI. Despite YnaI having additional transmembrane helices, important features are conserved, suggesting a common mechanism.