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首页> 外文期刊>Biochimica et biophysica acta. Biomembranes >Using a SMALP platform to determine a sub-nm single particle cryo-EM membrane protein structure
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Using a SMALP platform to determine a sub-nm single particle cryo-EM membrane protein structure

机译：使用Smalp平台来确定子NM单粒子冷冻膜蛋白结构

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Abstract The field of membrane protein structural biology has been revolutionized over the last few years with a number of high profile structures being solved using cryo-EM including Piezo, Ryanodine receptor, TRPV1 and the Glutamate receptor. Further developments in the EM field hold the promise of even greater progress in terms of greater resolution, which for membrane proteins is still typically within the 4–7? range. One advantage of a cryo-EM approach is the ability to study membrane proteins in more “native” like environments for example proteoliposomes, amphipols and nanodiscs. Recently, styrene maleic acid co-polymers (SMA) have been used to extract membrane proteins surrounded by native lipids (SMALPs) maintaining a more natural environment. We report here the structure of the Escherichia coli multidrug efflux transporter AcrB in a SMALP scaffold to sub-nm resolution, with the resulting map being consistent with high resolution crystal structures and other EM derived maps. However, both the C-terminal helix (TM12) and TM7 are poorly defined in the map. These helices are at the exterior of the helical bundle and form the greater interaction with the native lipids and SMA polymer and may represent a more dynamic region of the protein. This work shows the promise of using an SMA approach for single particle cryo-EM studies to provide sub-nm structures. Graphical abstract Display Omitted Highlights ? The first sub nm single particle reconstruction of a membrane protein using a SMALP scaffold ? The ability to maintain a native like environment for structural studies holds great promise. ? The resulting map is consistent with high resolution crystal structures and other EM derived maps.
机译：摘要膜蛋白结构生物学领域已经在过去几年中彻底改变了许多使用Cryo-EM在包括压电，瑞那胺受体，TRPV1和谷氨酸受体中解决的高轮廓结构。 EM场的进一步发展在更大的分辨率方面具有更高的进展，这对于膜蛋白通常仍然在4-7内？范围。冷冻热方法的一个优点是能够在更“天然”的环境中研究膜蛋白，例如蛋白聚体，Amphipols和纳米蛋白酶。最近，苯乙烯马来酸共聚物（SMA）已被用于提取由天然脂质（Smalps）包围的膜蛋白保持更自然的环境。我们在此报告将大肠杆菌的大肠杆菌MultiDrug Efflux输送器ACRB的结构在Smalp脚手架中到Sub-NM分辨率，得到的映射与高分辨率晶体结构和其他EM衍生图一致。但是，C终端螺旋（TM12）和TM7都在地图中定义不足。这些螺旋位于螺旋束的外部，形成与天然脂质和SMA聚合物的更大的相互作用，并且可以代表蛋白质的更动力区域。这项工作显示了使用SMA方法进行单粒子冷冻-EM研究的承诺，以提供子NM结构。图形抽象显示省略了亮点？使用Smalp支架的第一亚NM单颗粒重建膜蛋白？维持原生植物的结构性研究的能力具有很大的承诺。还得到的地图与高分辨率晶体结构和其他EM衍生图一致。

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