In molecular biology, the GGDEF domain is a protein domain which appears to be ubiquitous in bacteria and is often linked to a regulatory domain, such as a phosphorylation receiver or oxygen sensing domain. Its function is to act as a diguanylate cyclase and synthesize cyclic di-GMP, which is used as an intracellular signalling molecule in a wide variety of bacteria.[1][2] Enzymatic activity can be strongly influenced by the adjacent domains. Processes regulated by this domain include exopolysaccharide synthesis, biofilm formation, motility and cell differentiation.
| GGDEF domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 response regulator PleD in complex with c-diGMP | |||||||||
| Identifiers | |||||||||
| Symbol | GGDEF | ||||||||
| Pfam | PF00990 | ||||||||
| Pfam clan | CL0276 | ||||||||
| InterPro | IPR000160 | ||||||||
| SCOP2 | 1w25 / SCOPe / SUPFAM | ||||||||
| CDD | cd01949 | ||||||||
| |||||||||
Structural studies of PleD from Caulobacter crescentus show that this domain forms a five-stranded beta sheet surrounded by helices, similar to the catalytic core of adenylate cyclase.[3]
References
edit- ^ Paul R, Weiser S, Amiot NC, Chan C, Schirmer T, Giese B, Jenal U (March 2004). "Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain". Genes Dev. 18 (6): 715–27. doi:10.1101/gad.289504. PMC 387245. PMID 15075296.
- ^ Ryjenkov DA, Tarutina M, Moskvin OV, Gomelsky M (March 2005). "Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain". J. Bacteriol. 187 (5): 1792–8. doi:10.1128/JB.187.5.1792-1798.2005. PMC 1064016. PMID 15716451.
- ^ Chan C, Paul R, Samoray D, Amiot NC, Giese B, Jenal U, Schirmer T (December 2004). "Structural basis of activity and allosteric control of diguanylate cyclase". Proc. Natl. Acad. Sci. U.S.A. 101 (49): 17084–9. Bibcode:2004PNAS..10117084C. doi:10.1073/pnas.0406134101. PMC 535365. PMID 15569936.