Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Comment
. 2009 Aug;191(15):4697-700.
doi: 10.1128/JB.00651-09. Epub 2009 May 29.

Rationalizing the evolution of EAL domain-based cyclic di-GMP-specific phosphodiesterases

Ute Römling  1
Affiliations
Comment

Rationalizing the evolution of EAL domain-based cyclic di-GMP-specific phosphodiesterases

Ute Römling. J Bacteriol. 2009 Aug.
No abstract available

PubMed Disclaimer

Figures

FIG. 1.
FIG. 1.
Hydrolysis of c-di-GMP to linear guanylic acid 5′-pGpG is catalyzed by the enzymatic activity of phosphodiesterase A, which is conferred by EAL domains.
FIG. 2.
FIG. 2.
Alignment of signature motifs of functionally characterized class 1, 2, and 3 EAL domains. The proteins with class 1 EAL domains displayed showed c-di-GMP-specific PDE activity in vitro (1, 3, 17, 23, 30, 33). YhjH and YahA, which have class 2 EAL domains, display c-di-GMP-specific PDE activity (15, 23, 26), while this activity is lacking in YkuI and DGC2 (12, 28). Proteins with class 3 EAL domains lack c-di-GMP-specific PDE activity (13, 26, 27, 32). LapD, however, binds c-di-GMP (13). For further explanations, see text. RocR was used as a model to investigate the role of conserved residues on catalytic activity (17). Amino acids involved in Mg2+ binding are shown in green (light green, direct binding; dark green, indirectly involved); amino acids involved in substrate binding are shown in blue. The glutamate serving as the general base catalyst is shown in red, and the glutamate stabilizing loop 6 is shown in pink. The exchange of underlined amino acids by alanine led to >105-fold reduction in catalytic activity in RocR (17). Amino acids on gray background were mutagenized to study the role of loop 6 in RocR (16). Exchange of three amino acids (dark red and underlined in the sequence above the original loop 6 sequence) in loop 6 of the EAL domain of DGC2 restored the c-di-GMP-specific PDE activity (17). Underlined amino acids in LapD were demonstrated to participate in c-di-GMP binding (13).
See this image and copyright information in PMC

Comment on

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Barends, T. R. M., E. Hartmann, J. J. Griese, T. Beitlich, N. V. Kirienko, D. A. Ryjenkov, J. Reinstein, R. I. Shoeman, M. Gomelsky, and I. Schlichting. 2009. Structure and mechanism of a bacterial light-regulated cyclic nucleotide phosphodiesterase. Nature, 4591015-1018. - PubMed
    1. Bender, A. T., and J. A. Beavo. 2006. Cyclic nucleotide phosphodiesterases: molecular regulation to clinical use. Pharmacol. Rev. 58488-520. - PubMed
    1. Chang, A. L., J. R. Tuckerman, G. Gonzalez, R. Mayer, H. Weinhouse, G. Volman, D. Amikam, M. Benziman, and M. A. Gilles-Gonzalez. 2001. Phosphodiesterase A1, a regulator of cellulose synthesis in Acetobacter xylinum, is a heme-based sensor. Biochemistry 403420-3426. - PubMed
    1. Christen, M., B. Christen, M. Folcher, A. Schauerte, and U. Jenal. 2005. Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP. J. Biol. Chem. 28030829-30837. - PubMed
    1. Cotter, P. A., and S. Stibitz. 2007. c-di-GMP-mediated regulation of virulence and biofilm formation. Curr. Opin. Microbiol. 1017-23. - PubMed

Publication types

MeSH terms

LinkOut - more resources