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High-resolution structure of the major periplasmic domain from the cell shape-determining filament MreC

机译:从细胞形状决定丝MreC的主要周质结构的高分辨率结构

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Bacterial cell shape is dictated by the cell wall, a plastic structure that must adapt to growth and division whilst retaining its function as a selectively permeable barrier. The modulation of cell wall structure is achieved by a variety of enzymatic functions, all of which must be spatially regulated in a precise manner. The membrane-spanning essential protein MreC has been identified as the central hub in this process, linking the bacterial cytoskeleton to a variety of cell wall-modifying enzymes. Additionally, MreC can form filaments, believed to run perpendicularly to the membrane. We present here the 1.2 angstrom resolution crystal structure of the major periplasmic domain of Streptococcus pneumoniae MreC. The protein shows a novel arrangement of two barrel-shaped domains, one of which shows homology to a known protein oligomerization motif, with the other resembling a catalytic domain from a bacterial protease. We discuss the implications of these results for MreC function, and detail the structural features of the molecule that may be responsible for the binding of partner proteins. (c) 2007 Elsevier Ltd. All rights reserved.
机译:细菌细胞的形状由细胞壁决定,细胞壁是一种塑料结构,必须适应生长和分裂,同时保持其选择性渗透屏障的功能。细胞壁结构的调节是通过多种酶功能实现的,所有这些功能必须以精确的方式在空间上进行调节。跨膜必需蛋白MreC已被确定为该过程的中心枢纽,它将细菌细胞骨架与多种细胞壁修饰酶连接在一起。另外,MreC可以形成细丝,据信它们垂直于膜延伸。我们在这里介绍肺炎链球菌MreC的主要周质结构域的1.2埃分辨率晶体结构。该蛋白质显示出两个桶状结构域的新颖排列,其中一个与已知的蛋白质寡聚化基序具有同源性,另一个类似于细菌蛋白酶的催化结构域。我们讨论了这些结果对MreC功能的影响,并详细介绍了可能与伴侣蛋白结合的分子的结构特征。 (c)2007 Elsevier Ltd.保留所有权利。

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