MreC is a scaffold protein required for cell shape determination through interactions with proteins related to cell wall synthesis. Here, we determined the crystal structure of the major periplasmic part of MreC from Escherichia coli at 2.1 Å resolution. The periplasmic part of MreC contains a coiled-coil domain and two six-stranded barrel domains. The coiled-coil domain is essential for dimer formation, and the two monomers are prone to relative motion that is related to the small interface of β-barrel domains. In addition, MreC forms an antiparallel filament-like structure along the coiled-coil direction, which is different from the helical array structure in Pseudomonas aeruginosa. Our structure deepens our understanding of polymer formation of MreC.

中文翻译：

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MreC 的晶体结构提供了对聚合物形成的见解

MreC 是通过与与细胞壁合成相关的蛋白质相互作用来确定细胞形状所需的支架蛋白。在这里，我们以 2.1 Å 的分辨率确定了来自大肠杆菌的 MreC 主要周质部分的晶体结构。MreC 的周质部分包含一个卷曲螺旋结构域和两个六链桶结构域。卷曲螺旋结构域对于二聚体的形成是必不可少的，并且这两个单体易于发生与 β-桶结构域的小界面有关的相对运动。此外，MreC沿盘绕方向形成反平行的细丝状结构，与铜绿假单胞菌的螺旋排列结构不同。我们的结构加深了我们对 MreC 聚合物形成的理解。