Structural Insight into Partner Specificity and Phosphoryl Transfer in Two-Component Signal Transduction

被引:312
作者
Casino, Patricia
Rubio, Vicente
Marina, Alberto [1 ]
机构
[1] CSIC, IBV, Valencia 46010, Spain
关键词
HISTIDINE KINASE ENVZ; RESPONSE REGULATOR; ESCHERICHIA-COLI; CRYSTAL-STRUCTURE; SELENOMETHIONYL PROTEINS; MOLECULAR RECOGNITION; PHOSPHATASE-ACTIVITY; DOMAIN; SENSOR; COMPLEX;
D O I
10.1016/j.cell.2009.08.032
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The chief mechanism used by bacteria for sensing their environment is based on two conserved proteins: a sensor histidine kinase (HK) and an effector response regulator (RR). The signal transduction process involves highly conserved domains of both proteins that mediate autokinase, phospho-transfer, and phosphatase activities whose output is a finely tuned RR phosphorylation level. Here, we report the structure of the complex between the entire cytoplasmic portion of Thermotoga maritima class I HK853 and its cognate, RR468, as well as the structure of the isolated RR468, both free and BeF3- bound. Our results provide insight into partner specificity in two-component systems, recognition of the phosphorylation state of each partner, and the catalytic mechanism of the phosphatase reaction. Biochemical analysis shows that the HK853-catalyzed autokinase reaction proceeds by a cis autophosphorylation mechanism within the HK subunit. The results suggest a model for the signal transduction mechanism in two-component systems.
引用
收藏
页码:325 / 336
页数:12
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