...
首页> 外文期刊>Journal of synchrotron radiation >Crystal structure of the N-terminal domain of MinC dimerized via domain swapping
【24h】

Crystal structure of the N-terminal domain of MinC dimerized via domain swapping

机译:MinC N末端结构域的晶体结构通过结构域交换而二聚化

获取原文
获取原文并翻译 | 示例
           

摘要

Proper cell division at the mid-site of gram-negative bacteria reflects critical regulation by the min system (MinC, MinD and MinE) of the cytokinetic Z ring, which is a polymer composed of FtsZ subunits. MinC and MinD act together to inhibit aberrantly positioned Z-ring formation. MinC consists of two domains: an N-terminal domain (MinCNTD), which interacts with FtsZ and inhibits FtsZ polymerization, and a C-terminal domain (MinCCTD), which interacts with MinD and inhibits the bundling of FtsZ filaments. These two domains reportedly function together, and both are essential for normal cell division. The full-length dimeric structure of MinC from Thermotoga maritima has been reported, and shows that MinC dimerization occurs via MinCCTD; MinCNTD is not involved in dimerization. Here the crystal structure of Escherichia coli MinCNTD (EcoMinCNTD) is reported. EcoMinCNTD forms a dimer via domain swapping between the first β strands in each subunit. It is therefore suggested that the dimerization of full-length EcoMinC occurs via both MinCCTD and MinCNTD, and that the dimerized EcoMinCNTD likely plays an important role in inhibiting aberrant Z-ring localization.
机译:革兰氏阴性细菌中位的适当细胞分裂反映了细胞动力学Z环的min系统(MinC,MinD和MinE)的关键调节作用,该系统是由FtsZ亚基组成的聚合物。 MinC和MinD共同作用以抑制异常定位的Z形环的形成。 MinC由两个域组成:一个N末端域(MinCNTD)与FtsZ相互作用并抑制FtsZ聚合,一个C末端域(MinCCTD)与MinD相互作用并抑制FtsZ丝束。据报道这两个结构域一起起作用,并且对于正常细胞分裂都是必不可少的。已经报道了来自滨海嗜热菌的MinC的全长二聚体结构,并且表明MinC二聚化通过MinCCTD发生。 MinCNTD不参与二聚化。此处报道了大肠杆菌MinCNTD(EcoMinCNTD)的晶体结构。 EcoMinCNTD通过每个亚基中第一个β链之间的结构域交换形成二聚体。因此,建议全长EcoMinC的二聚化通过MinCCTD和MinCNTD发生,并且二聚化的EcoMinCNTD可能在抑制异常Z环定位中起重要作用。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号