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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Crystal structure of a photoactivated deprotonated intermediate of rhodopsin
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Crystal structure of a photoactivated deprotonated intermediate of rhodopsin

机译：视紫红质光活化去质子化中间体的晶体结构

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摘要

The changes that lead to activation of G protein-coupled receptors have not been elucidated at the structural level. In this work we report the crystal structures of both ground state and a photoactivated deprotonated intermediate of bovine rhodopsin at a resolution of 4.15 angstrom. in the photoactivated state, the Schiff base linking the chromophore and Lys-296 becomes deprotonated, reminiscent of the G protein-activating state, metarhodopsin II. The structures reveal that the changes that accompany photoactivation are smaller than previously predicted for the metarhodopsin 11 state and include changes on the cytoplasmic surface of rhodopsin that possibly enable the coupling to its cognate G protein, transducin. Furthermore, rhodopsin forms a potentially physiologically relevant dimer interface that involves helices 1, 11, and 8, and when taken with the prior work that implicates helices IV and V as the physiological dimer interface may account for one of the interfaces of the oligomeric structure of rhodopsin seen in the membrane by atomic force microscopy. The activation and oligomerization models likely extend to the majority of other G protein-coupled receptors. G
机译：在结构水平上尚未阐明导致G蛋白偶联受体活化的变化。在这项工作中，我们报告了牛视紫红质的基态和光活化去质子化中间体的晶体结构，分辨率为4.15埃。在光激活状态下，连接发色团和Lys-296的席夫碱变得去质子化，让人联想到G蛋白激活状态即视紫红质II。该结构表明，伴随光激活的变化比原先的视紫红质11状态所预测的要小，并且包括视紫红质在细胞质表面的变化，这可能使其与其相关的G蛋白转导蛋白偶联。此外，视紫红质形成潜在的生理学相关的二聚体界面，其涉及螺旋1、11和8，并且当涉及暗示螺旋IV和V的现有工作时，由于生理二聚体界面可解释了寡聚体结构的界面之一。通过原子力显微镜在膜中观察到了视紫红质。激活和低聚模型可能扩展到大多数其他G蛋白偶联受体。 G

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