Crystal structure of the Z-ring associated cell division protein ZapC from Escherichia coli.
Crystal structure of the Z-ring associated cell division protein ZapC from Escherichia coli.
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DOI：
10.1016/j.febslet.2015.11.030
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发表时间：
2015-12-21
期刊：
影响因子：
3.5
通讯作者：
Löwe J
中科院分区：
文献类型：
--
作者：
Ortiz C;Kureisaite-Ciziene D;Schmitz F;McLaughlin SH;Vicente M;Löwe J
首先解决了细菌细胞分裂调节剂ZapC的晶体结构问题。ZapC是一种双域蛋白，与Tudor和chromo结构域有相似之处。ZapC以中等亲和力结合FtsZ的C-末端。细菌细胞分裂涉及一个收缩环，该环在分裂部位组织下游蛋白质，并包含微管蛋白同源物FtsZ。ZapC被发现是FtsZ的非必需调节因子。它定位于隔环，zapC的缺失导致轻微的表型，而过度表达则抑制细胞分裂。与FtsZ的相互作用促进了对细胞分裂的干扰。在这里，我们介绍了从大肠杆菌中提取的ZapC的2.9°晶体结构。ZapC形成一个二聚体，由两个结构域组成，这两个结构域属于皇家超家族，其中许多成员与甲基化精氨酸或赖氨酸结合。ZapC含有N-末端类似铬的结构域和类似Tudor的C-末端结构域。ITC结果表明，ZapC与FtsZ的C-末端结合。
First crystal structure of bacterial cell division regulator ZapC solved. ZapC is a two-domain protein, with similarities to Tudor and chromo domains. ZapC binds the C-terminal tail of FtsZ with moderate affinity. Bacterial cell division involves a contractile ring that organises downstream proteins at the division site and which contains the tubulin homologue FtsZ. ZapC has been discovered as a non-essential regulator of FtsZ. It localises to the septal ring and deletion of zapC leads to a mild phenotype, while overexpression inhibits cell division. Interference with cell division is facilitated by an interaction with FtsZ. Here, we present the 2.9 Å crystal structure of ZapC from Escherichia coli. ZapC forms a dimer and comprises two domains that belong to the Royal superfamily of which many members bind methylated arginines or lysines. ZapC contains an N-terminal chromo-like domain and a Tudor-like C-terminal domain. We show by ITC that ZapC binds the C-terminal tail of FtsZ.