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Projection map of aquaporin-9 at 7 A resolution.

机译:Aquaporin-9在7 A分辨率下的投影图。

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摘要

Aquaporin-9, an aquaglyceroporin present in diverse tissues, is unique among aquaporins because it is not only permeable to water, urea and glycerol, but also allows passage of larger uncharged solutes. Single particle analysis of negatively stained recombinant rat aquaporin-9 revealed a particle size characteristic of the tetrameric organization of all members of the aquaporin family. Reconstitution of aquaporin-9 into two-dimensional crystals enabled us to calculate a projection map at 7 A resolution. The projection structure indicates a tetrameric structure, similar to GlpF, with each square-like monomer forming a pore. A comparison of the pore-lining residues between the crystal structure of GlpF and a homology model of aquaporin-9 locates substitutions in these residues predominantly to the hydrophobic edge of the tripathic pore of GlpF, providing first insights into the structural basis for the broader substrate specificity of aquaporin-9.
机译:Aquaporin-9是存在于多种组织中的一种水甘油糖蛋白,在水瓷蛋白中是独特的,因为它不仅可渗透水,尿素和甘油,而且还允许较大的不带电荷的溶质通过。阴性染色的重组大鼠水通道蛋白9的单颗粒分析揭示了水通道蛋白家族所有成员四聚体组织的粒径特征。将aquaporin-9重构为二维晶体,​​使我们能够计算出7 A分辨率的投影图。突出结构表示类似于GlpF的四聚体结构,每个正方形单体形成孔。比较GlpF的晶体结构和aquaporin-9的同源性模型之间的孔衬残基,发现这些残基中的取代主要位于GlpF的三态孔的疏水边缘,从而为更广泛的底物的结构基础提供了初步见解水通道蛋白9的特异性。

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