| 词条 | GGDEF domain |
| 释义 |
| Symbol = GGDEF | Name = GGDEF domain | image = PDB 1w25 EBI.jpg | width = | caption = response regulator PleD in complex with c-diGMP | Pfam = PF00990 | Pfam_clan = CL0276 | InterPro = IPR000160 | SMART = | PROSITE = | MEROPS = | SCOP = 1w25 | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = cd01949 }} 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. 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]References1. ^{{cite journal |vauthors=Paul R, Weiser S, Amiot NC, Chan C, Schirmer T, Giese B, Jenal U | title = Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain | journal = Genes Dev. | volume = 18 | issue = 6 | pages = 715–27 |date=March 2004 | pmid = 15075296 | pmc = 387245 | doi = 10.1101/gad.289504 | url = }} {{InterPro content|IPR000160}}{{Protein domains}}2. ^{{cite journal |vauthors=Ryjenkov DA, Tarutina M, Moskvin OV, Gomelsky M | title = Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain | journal = J. Bacteriol. | volume = 187 | issue = 5 | pages = 1792–8 |date=March 2005 | pmid = 15716451 | pmc = 1064016 | doi = 10.1128/JB.187.5.1792-1798.2005 | url = }} 3. ^{{cite journal |vauthors=Chan C, Paul R, Samoray D, Amiot NC, Giese B, Jenal U, Schirmer T | title = Structural basis of activity and allosteric control of diguanylate cyclase | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 101 | issue = 49 | pages = 17084–9 |date=December 2004 | pmid = 15569936 | pmc = 535365 | doi = 10.1073/pnas.0406134101 | url = }} 1 : Protein domains |
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