Crystal structures of YfiR from Pseudomonas aeruginosa in two redox states
Crystal structures of YfiR from Pseudomonas aeruginosa in two redox states
复制标题
两种氧化还原态的铜绿假单胞菌 YfiR 晶体结构。
DOI：
10.1016/j.bbrc.2015.03.160
复制
发表时间：
2015-05-22
影响因子：
3.1
通讯作者：
Jiang, Tao
中科院分区：
文献类型：
--
作者：
Yang, Xuan;Yang, Xiu-an;Jiang, Tao
YfiBNR是最近发现的参与细菌生物膜形成的c-di-GMP调控系统。外质蛋白YfiR抑制内膜蛋白YfiN的二胍酸环化酶活性，而外膜中的YfiB可以通过隔离YfiR来释放这种抑制作用。此外，该系统可能通过YfiR响应缺氧条件，尽管详细机制尚不清楚。在这里，我们报告了铜绿假单胞菌YfiR在氧化谷胱甘肽缺失和存在下的晶体结构。我们的结构首次揭示了YfiR的整体折叠，并证明了YfiR以二聚体的形式存在。比较两种结构在不同氧化还原状态下的结构，发现一个二硫键（Cys71-Cys110）断裂/形成，另一个二硫键（Cys145-Cys152）周围发生局部构象变化。诱变研究表明，Cys145-Cys152在维持YfiR正确折叠中起重要作用。(C) 2015爱思唯尔公司版权所有。
YfiBNR is a recently identified c-di-GMP regulatory system involved in bacterial biofilm formation. The periplasmic protein YfiR inhibits the diguanylate cyclase activity of the inner membrane protein YfiN, whereas YfiB in the outer membrane can release this inhibition by sequestration of YfiR. In addition, this system may respond to anoxic conditions via YfiR, although the detailed mechanism is still unknown. Here we report crystal structures of Pseudomonas aeruginosa YfiR in the absence and presence of oxidative glutathione. Our structures reveal the overall folding of YfiR for the first time and demonstrate that YfiR exist as a dimer. Comparison of the two structures in different redox states revealed a broken/formation of one disulfide bond (Cys71-Cys110) and local conformational change around the other one (Cys145-Cys152). Mutagenesis studies indicated that Cys145-Cys152 plays an important role in maintaining the correct folding of YfiR. (C) 2015 Elsevier Inc. All rights reserved.