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首页> 外文期刊>EMBO Journal >High-resolution AFM topographs of Rubrivivax gelatinosus light-harvesting complex LH2.
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High-resolution AFM topographs of Rubrivivax gelatinosus light-harvesting complex LH2.

机译:高分辨率AFM Rubrivivax x射线物相照片LH2 gelatinosus聚光复杂。

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摘要

Light-harvesting complexes 2 (LH2) are the accessory antenna proteins in the bacterial photosynthetic apparatus and are built up of alphabeta-heterodimers containing three bacteriochlorophylls and one carotenoid each. We have used atomic force microscopy (AFM) to investigate reconstituted LH2 from Rubrivivax gelatinosus, which has a C-terminal hydrophobic extension of 21 amino acids on the alpha-subunit. High-resolution topographs revealed a nonameric organization of the regularly packed cylindrical complexes incorporated into the membrane in both orientations. Native LH2 showed one surface which protruded by approximately 6 A and one that protruded by approximately 14 A from the membrane. Topographs of samples reconstituted with thermolysin-digested LH2 revealed a height reduction of the strongly protruding surface to approximately 9 A, and a change of its surface appearance. These results suggested that the alpha-subunit of R.gelatinosus comprises a single transmembrane helix and an extrinsic C-terminus, and allowed the periplasmic surface to be assigned. Occasionally, large rings ( approximately 120 A diameter) surrounded by LH2 rings were observed. Their diameter and appearance suggest the large rings to be LH1 complexes.
机译:聚光配合物2 (LH2)辅助天线在细菌蛋白质光合机构的建立alphabeta-heterodimers包含三个细菌叶绿素和类胡萝卜素。用原子力显微镜(AFM)调查从Rubrivivax重组LH2gelatinosus, c端疏水扩展alpha-subunit 21个氨基酸。高分辨率x射线物相照片揭示了nonameric组织定期的圆柱形包装配合物组成的膜取向。伸出了大约6,另一个黑洞洞的大约14个膜。与thermolysin-digested LH2显示高度减少强烈突出表面大约9,改变其表面外观。alpha-subunit R.gelatinosus由单一跨膜螺旋和一个外在糖基,并允许周质的表面分配。大约120直径)LH2包围戒指被观察到。外观显示LH1大环复合物。

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