Volume 7 Issue 6
Jun.  2016
Turn off MathJax
Article Contents
Min Xu, Xuan Yang, Xiu-An Yang, Lei Zhou, Tie-Zheng Liu, Zusen Fan, Tao Jiang. Structural insights into the regulatory mechanism of the Pseudomonas aeruginosa YfiBNR system[J]. Protein&Cell, 2016, 7(6): 403-416. doi: 10.1007/s13238-016-0264-7
Citation: Min Xu, Xuan Yang, Xiu-An Yang, Lei Zhou, Tie-Zheng Liu, Zusen Fan, Tao Jiang. Structural insights into the regulatory mechanism of the Pseudomonas aeruginosa YfiBNR system[J]. Protein&Cell, 2016, 7(6): 403-416. doi: 10.1007/s13238-016-0264-7

Structural insights into the regulatory mechanism of the Pseudomonas aeruginosa YfiBNR system

doi: 10.1007/s13238-016-0264-7
Funds:

This work was supported by grants from the National Natural Science Foundation of China (Grant Nos. 31570768 and 91419308) and the Strategic Priority Research Program (XDB08010301).

  • Received Date: 2016-02-17
  • Rev Recd Date: 2016-03-10
  • YfiBNR is a recently identified bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) signaling system in opportunistic pathogens. It is a key regulator of biofilm formation, which is correlated with prolonged persistence of infection and antibiotic drug resistance. In response to cell stress, YfiB in the outer membrane can sequester the periplasmic protein YfiR, releasing its inhibition of YfiN on the inner membrane and thus provoking the diguanylate cyclase activity of YfiN to induce c-di-GMP production. However, the detailed regulatory mechanism remains elusive. Here, we report the crystal structures of YfiB alone and of an active mutant YfiBL43P complexed with YfiR with 2:2 stoichiometry. Structural analyses revealed that in contrast to the compact conformation of the dimeric YfiB alone, YfiBL43P adopts a stretched conformation allowing activated YfiB to penetrate the peptidoglycan (PG) layer and access YfiR. YfiBL43P shows a more compact PG-binding pocket and much higher PG binding affinity than wild-type YfiB, suggesting a tight correlation between PG binding and YfiB activation. In addition, our crystallographic analyses revealed that YfiR binds Vitamin B6 (VB6) or L-Trp at a YfiB-binding site and that both VB6 and L-Trp are able to reduce YfiBL43P-induced biofilm formation. Based on the structural and biochemical data, we propose an updated regulatory model of the YfiBNR system.
  • loading
  • 加载中

Catalog

    通讯作者: 陈斌, bchen63@163.com
    • 1. 

      沈阳化工大学材料科学与工程学院 沈阳 110142

    1. 本站搜索
    2. 百度学术搜索
    3. 万方数据库搜索
    4. CNKI搜索

    Article Metrics

    Article views (311) PDF downloads(1901) Cited by()
    Proportional views
    Related

    /

    DownLoad:  Full-Size Img  PowerPoint
    Return
    Return