南方科技大学知识苑(SUSTech KC): Structural basis for diguanylate cyclase activation by its binding partner in pseudomonas aeruginosa

题名	Structural basis for diguanylate cyclase activation by its binding partner in pseudomonas aeruginosa
作者	Chen，Gukui 1; Zhou，Jiashen 2; Zuo，Yili 1; Huo，Weiping 1; Peng，Juan 1; Li，Meng 1; Zhang，Yani 1; Wang，Tietao 1; Zhang，Lin 2; Zhang，Liang 2; Liang，Haihua1,3
通讯作者	Zhang，Liang; Liang，Haihua
发表日期	2021-09-01
DOI	10.7554/eLife.67289
发表期刊	eLife 影响因子和分区
EISSN	2050-084X
卷号	10
摘要	Cyclic-di-guanosine monophosphate (c-di-GMP) is an important effector associated with acute-chronic infection transition in Pseudomonas aeruginosa. Previously, we reported a signaling network SiaABCD, which regulates biofilm formation by modulating c-di-GMP level. However, the mechanism for SiaD activation by SiaC remains elusive. Here we determine the crystal structure of SiaC-SiaD-GpCpp complex and revealed a unique mirror symmetric conformation: two SiaD form a dimer with long stalk domains, while four SiaC bind to the conserved motifs on the stalks of SiaD and stabilize the conformation for further enzymatic catalysis. Furthermore, SiaD alone exhibits an inactive pentamer conformation in solution, demonstrating that SiaC activates SiaD through a dynamic mechanism of promoting the formation of active SiaD dimers. Mutagenesis assay confirmed that the stalks of SiaD are necessary for its activation. Together, we reveal a novel mechanism for DGC activation, which clarifies the regulatory networks of c-di-GMP signaling.
相关链接	[Scopus记录]
收录类别	SCI
语种	英语
学校署名	通讯
资助项目	National Natural Science Foundation of China[21722802];National Natural Science Foundation of China[31700064];National Natural Science Foundation of China[31870060];National Natural Science Foundation of China[32170188];National Natural Science Foundation of China[91853118];
WOS记录号	WOS:000700397200001
Scopus记录号	2-s2.0-85116310076
来源库	Scopus
引用统计	被引频次[WOS]：7
成果类型	期刊论文
条目标识符	http://sustech.caswiz.com/handle/2SGJ60CL/382641
专题	南方科技大学医学院
作者单位	1.Key Laboratory of Resources Biology and Biotechnology in Western China,Ministry of Education,College of Life Sciences,Northwest University,ShaanXi,China 2.Department of Pharmacology and Chemical Biology,Shanghai Jiao Tong University,School of Medicine,Shanghai,China 3.School of Medicine,Southern University of Science and Technology,Shenzhen,China
通讯作者单位	南方科技大学医学院
推荐引用方式 GB/T 7714	Chen，Gukui,Zhou，Jiashen,Zuo，Yili,et al. Structural basis for diguanylate cyclase activation by its binding partner in pseudomonas aeruginosa[J]. eLife,2021,10.
APA	Chen，Gukui.,Zhou，Jiashen.,Zuo，Yili.,Huo，Weiping.,Peng，Juan.,...&Liang，Haihua.(2021).Structural basis for diguanylate cyclase activation by its binding partner in pseudomonas aeruginosa.eLife,10.
MLA	Chen，Gukui,et al."Structural basis for diguanylate cyclase activation by its binding partner in pseudomonas aeruginosa".eLife 10(2021).