Structural highlights
Function
PDEL_ECOLI Acts both as an enzyme and as a c-di-GMP sensor to couple transcriptional activity to the c-di-GMP status of the cell (PubMed:26553851). Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG (PubMed:15995192, PubMed:24451384, PubMed:26553851). Also acts as a transcription factor to control its own expression (PubMed:26553851).[1] [2] [3]
References
- ↑ Schmidt AJ, Ryjenkov DA, Gomelsky M. The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains. J Bacteriol. 2005 Jul;187(14):4774-81. PMID:15995192 doi:http://dx.doi.org/187/14/4774
- ↑ Sundriyal A, Massa C, Samoray D, Zehender F, Sharpe T, Jenal U, Schirmer T. Inherent regulation of EAL domain-catalyzed hydrolysis of second messenger c-di-GMP. J Biol Chem. 2014 Jan 22. PMID:24451384 doi:http://dx.doi.org/10.1074/jbc.M113.516195
- ↑ Reinders A, Hee CS, Ozaki S, Mazur A, Boehm A, Schirmer T, Jenal U. Expression and Genetic Activation of Cyclic Di-GMP-Specific Phosphodiesterases in Escherichia coli. J Bacteriol. 2015 Nov 9;198(3):448-62. doi: 10.1128/JB.00604-15. PMID:26553851 doi:http://dx.doi.org/10.1128/JB.00604-15
