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首页> 外文期刊>Journal of Molecular Biology >Structure of the major membrane protein complex from urinary bladder epithelial cells by cryo-electron crystallography.
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Structure of the major membrane protein complex from urinary bladder epithelial cells by cryo-electron crystallography.

机译：冷冻上皮电子晶体学分析膀胱上皮细胞主要膜蛋白复合物的结构。

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摘要

Numerous protein plaques cover the apical surface of mammalian urinary bladder epithelial cells. These plaques contain four integral membrane proteins, called uroplakins, which form a well-ordered array of hexameric complexes. The 3D structure of these naturally occurring 2D crystals was studied by cryo-electron-crystallographic methods using a slow-scan charged-coupled device (CCD) camera to record the electron micrographs. A 1.2 nm projection map calculated from untilted crystals shows that each hexamer comprises a ring of six inner and six outer domains at a radius of 5.7 nm and 9.2 nm respectively. The 3D structure shows that the mass is distributed strongly asymmetrically with respect to the membrane, with most of the mass protruding from the luminal face. Both domains in the asymmetric unit traverse the membrane and protrude from the membrane on the cytoplasmic side. On the luminal side, the two domains are bridged forming a stretched arc. The total thickness of the complex is about 13.2 nm. A model of the urothelial plaque reveals that contacts between the hexamers are much less extended than within the hexamers.
机译：大量蛋白斑覆盖哺乳动物膀胱上皮细胞的顶表面。这些噬菌斑包含四个完整的膜蛋白，称为uroplakins，它们形成排列整齐的六聚体复合物阵列。这些自然存在的2D晶体的3D结构通过使用慢扫描电荷耦合器件（CCD）相机的低温电子晶体学方法进行了研究，以记录电子显微照片。由结晶晶体计算出的1.2 nm投影图显示，每个六聚体均包含一个分别具有5.7 nm和9.2 nm半径的六个内部域和六个外部域的环。 3D结构显示质量相对于膜强烈不对称地分布，大部分质量从腔表面突出。不对称单元中的两个结构域都穿过膜并从细胞质侧的膜突出。在腔侧，两个区域桥接形成拉伸弧。络合物的总厚度为约13.2nm。尿路上皮斑块的模型显示，六聚体之间的接触比六聚体内部的接触少得多。

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