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首页> 外文期刊>Journal of Molecular Biology >Molecular organization of bovine rod cGMP-phosphodiesterase 6
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Molecular organization of bovine rod cGMP-phosphodiesterase 6

机译：牛杆cGMP-磷酸二酯酶6的分子组织

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摘要

Phosphodiesterase 6 (PDE6), a multisubunit (alpha beta gamma (2)delta) enzyme, plays a major role in visual function by hydrolysing cGMP in response to a light stimulus. Solubilized bovine rod PDE6 molecules depleted of their gamma subunits were purified to homogeneity from bovine retinal rods and their molecular organization was investigated by electron microscopy. Image analysis of single particles revealed the three-dimensional dimeric arrangement of the purified alpha beta delta complex, and the internal organization of each catalytic subunit into three distinct domains at a resolution of 2.8 nm. The relative volume of each domain is consistent with sequence analysis and functional data, which suggest that these domains correspond to the catalytic and two CAF domains. This hypothesis was confirmed by immunolabelling experiments, which located the N-terminal part of the catalytic subunit where the major interaction between the two alpha beta subunits was found to occur. The 3D molecular organization of human platelet PDE5 appears highly homologous to that of bovine rod PDE6, as predicted by similarities in their primary sequences. These observations describe the quaternary organization of the catalytic PDE6 ccp complex, and place the catalytic and regulatory domains on a structural model.
机译：磷酸二酯酶6（PDE6）是一种多亚基（alpha beta gamma（2）delta）酶，通过响应光刺激而水解cGMP，从而在视觉功能中发挥重要作用。从牛视网膜棒中纯化去除了其γ亚基的可溶牛棒PDE6分子，使其同质，并通过电子显微镜研究其分子结构。单个颗粒的图像分析显示了纯化的α-βδ复合物的三维二聚体排列，每个催化亚基的内部组织都以2.8 nm的分辨率分为三个不同的域。每个结构域的相对体积与序列分析和功能数据一致，这表明这些结构域对应于催化结构域和两个CAF结构域。免疫标记实验证实了这一假设，该实验位于催化亚基的N端，发现两个αβ亚基之间发生了主要相互作用。如其主要序列的相似性所预测，人血小板PDE5的3D分子组织似乎与牛杆PDE6的组织高度同源。这些观察结果描述了催化PDE6 ccp配合物的四级组织，并将催化域和调节域置于结构模型上。

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