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首页> 外文期刊>Journal of Molecular Biology >The Escherichia coli cell division protein and model Tat substrate SufI (FtsP) localizes to the septal ring and has a multicopper oxidase-like structure.
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The Escherichia coli cell division protein and model Tat substrate SufI (FtsP) localizes to the septal ring and has a multicopper oxidase-like structure.

机译：大肠杆菌细胞分裂蛋白和模型Tat底物SufI（FtsP）定位在间隔环上，并具有类似多铜氧化酶的结构。

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摘要

The Escherichia coli protein SufI (FtsP) has recently been proposed to be a component of the cell division apparatus. The SufI protein is also in widespread experimental use as a model substrate in studies of the Tat (twin arginine translocation) protein transport system. We have used SufI-GFP (green fluorescent protein) fusions to show that SufI localizes to the septal ring in the dividing cell. We have also determined the structure of SufI by X-ray crystallography to a resolution of 1.9 A. SufI is structurally related to the multicopper oxidase superfamily but lacks metal cofactors. The structure of SufI suggests it serves a scaffolding rather than an enzymatic role in the septal ring and reveals regions of the protein likely to be involved in the protein-protein interactions required to assemble SufI at the septal ring.
机译：大肠杆菌蛋白SufI（FtsP）最近被提议作为细胞分裂装置的组成部分。 SufI蛋白也被广泛用作Tat（双精氨酸易位）蛋白转运系统研究的模型底物。我们已使用SufI-GFP（绿色荧光蛋白）融合物来显示SufI定位于分裂细胞中的隔环。我们还通过X射线晶体学确定了SufI的结构，分辨率为1.9A。SufI在结构上与多铜氧化酶超家族有关，但缺乏金属辅因子。 SufI的结构表明，它在间隔环中起着支架作用而不是酶的作用，并揭示了可能与在间隔环上组装SufI所需的蛋白质-蛋白质相互作用有关的蛋白质区域。

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