GGDEF domain

Ausmees N., Mayer R., Weinhouse H., Volman G., Amikam D., Benziman M., and Lindberg M. 2001. Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity. FEMS Microbiol Lett 204 163-167. 

Curli fimbriae, electron microscopy, environmental conditions, Escherichia coli, GGDEF domain, ompR, regulation, rpoS, Salmonella typhimurium, thin aggregative fimbriae. 

By sequence similarity in combination with molecular modeling, the GGDEF domain has been suggested to confer nucleotide cyclization activity (Pei and Grishin 2001), but this function has to be experimentally proven. However, it is not very far fetched to speculate that the GGDEF domain might synthesize the cyclic nucleotide c-di-GMP, which has been identified as the allosteric activator for cellulose biosynthesis in G. xylinus (Ross et al. 1991). 

Pei J. and Grishin N.V. 2001. GGDEF domain is homologous to adenylyl cyclase. Proteins 42 210-216. 

We have discovered too that some relatives of FixL are able to translate information about O2 binding into different types of chemistries. Examples of this are a class of cyclase enzymes (called GGDEF domain cyclases) that synthesize cyclic nucleotides and a set of phosphodiesterase enzymes (called EAL domain phosphodiesterases) that can cleave these cyclic nucleotides. These enzymes, which are inti-... 

DUF1 Domain of unknown function with GGDEF motif B 0(0) 0(0) ... 

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