3GL9

The structure of a histidine kinase-response regulator complex sheds light into two-component signaling and reveals a novel cis autophosphorylation mechanism

Summary for 3GL9

• Entry DOI: 10.2210/pdb3gl9/pdb
• Descriptor: Response regulator, MAGNESIUM ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: beta-sheet, surrounded by alpha helices, both sides, signaling protein
• Biological source: Thermotoga maritima
• Total number of polymer chains: 4
• Total formula weight: 56230.56

Authors

Casino, P.,Rubio, V.,Marina, A. (deposition date: 2009-03-11, release date: 2009-10-27, Last modification date: 2024-11-20)

Primary citation

Casino, P.,Rubio, V.,Marina, A.
Structural Insight into Partner Specificity and Phosphoryl Transfer in Two-Component Signal Transduction
Cell(Cambridge,Mass.), 139:325-336, 2009

PubMed Abstract: 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, phosphotransfer, 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 BeF(3)(-) 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.

PubMed: 19800110
DOI: 10.1016/j.cell.2009.08.032

Experimental method

X-RAY DIFFRACTION (1.8 Å)