Structure of the Drosophila melanogaster Rab6 GTPase at 1.4 Å resolution.
Structure of the Drosophila melanogaster Rab6 GTPase at 1.4 Å resolution.
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果蝇 Rab6 GTPase 的结构，分辨率为 1.4 ×。
DOI：
10.1107/s1744309111017453
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发表时间：
2011
期刊：
影响因子：
--
通讯作者：
Walden M
中科院分区：
文献类型：
--
作者：
Walden M
Rab 6是属于p21 Ras超家族的一个小的GT3。它参与真核生物中高尔基体和内体/ER之间的囊泡运输。当核苷酸被交换为GTP时，GDP结合的无活性蛋白质经历构象变化，允许Rab 6与各种不同的效应蛋白相互作用。为了进一步了解这些变化如何影响下游蛋白质结合，来自黑腹果蝇的Rab 6的晶体结构已经被解析到1.4 μ m分辨率，这是迄今为止Rab 6结构的最高分辨率。 晶体属C2空间群，晶胞参数a = 116.5，B = 42.71，c = 86.86 °，α = 90，β = 133.12，γ = 90°。 该模型被细化为14.5%的R因子和17.3%的Rfree。
Rab6 is a small GTPase that belongs to the p21 Ras superfamily. It is involved in vesicle trafficking between the Golgi apparatus and endosomes/ER in eukaryotes. The GDP-bound inactive protein undergoes conformational changes when the nucleotide is exchanged to GTP, allowing Rab6 to interact with a variety of different effector proteins. To further understand how these changes affect downstream protein binding, the crystal structure of Rab6 from Drosophila melanogaster has been solved to 1.4 Å resolution, the highest resolution for a Rab6 structure to date. The crystals belonged to space group C2, with unit-cell parameters a = 116.5, b = 42.71, c = 86.86 Å, α = 90, β = 133.12, γ = 90°. The model was refined to an R factor of 14.5% and an Rfree of 17.3%.