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首页> 外文期刊>Acta crystallographica.Section D Biological crystallography. >Structure of the N-terminal domain of the effector protein LegC3 from Legionella pneumophila
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Structure of the N-terminal domain of the effector protein LegC3 from Legionella pneumophila

机译：n端结构域的结构效应蛋白质LegC3嗜肺性军团菌

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摘要

Legionella pneumophila secretes over 300 effectors during the invasion of human cells. The functions of only a small number of them have been identified. LegC3 is one of the identified effectors, which is believed to act by inhibiting vacuolar fusion. It contains two predicted transmembrane helices that divide the protein into a larger N-terminal domain and a smaller C-terminal domain. The function of LegC3 has been shown to be associated primarily with the N-terminal domain, which contains coiled-coil sequence motifs. The structure of the N-terminal domain has been determined and it is shown that it is highly α-helical and contains a helical bundle followed by a long antiparallel coiled-coil. No similar protein fold has been observed in the PDB. A long loop at the tip of the coiled-coil distal from the membrane is disordered and may be important for interaction with an as yet unidentified protein.
机译：嗜肺性军团菌分泌超过300效应器在人类细胞的入侵。只有少数人识别。效应器,相信通过抑制空泡的融合。把蛋白跨膜螺旋成一个更大的n端结构域和一个更小的c端域。显示主要与有关n端结构域,它包含卷曲螺旋序列图案。域已经确定和显示它是高度α螺旋和包含一个螺旋包长反平行的紧随其后卷曲螺旋。PDB中观察到。从膜的卷曲螺旋远端无序和可能重要的交互用一个未知的蛋白质。

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