Literature summary for 2.7.7.65 extracted from

Chan, C.; Paul, R.; Samoray, D.; Amiot, N.C.; Giese, B.; Jenal, U.; Schirmer, T.
Structural basis of activity and allosteric control of diguanylate cyclase (2004), Proc. Natl. Acad. Sci. USA, 101, 17084-17089.

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with product cyclic diguanylate. The guanine base is H-bonded to N335 and D344, whereas the ribosyl and alpha-phosphate moieties extend over the beta2-beta3-hairpin that carries the GGEEF signature motif. In the crystal, cyclic diguanylate molecules are crosslinking active sites of adjacent dimers. In solution, two diguanylate cyclase doamins of a dimer may align in a twofold symmetric way to catalyze synthesis of cyclic diguanylate	Caulobacter vibrioides

Crystallization (Comment)

Organism

in complex with product cyclic diguanylate. The guanine base is H-bonded to N335 and D344, whereas the ribosyl and alpha-phosphate moieties extend over the beta2-beta3-hairpin that carries the GGEEF signature motif. In the crystal, cyclic diguanylate molecules are crosslinking active sites of adjacent dimers. In solution, two diguanylate cyclase doamins of a dimer may align in a twofold symmetric way to catalyze synthesis of cyclic diguanylate

Caulobacter vibrioides

Inhibitors

Inhibitors	Comment	Organism	Structure
cyclic 3',5'-diguanylate	product inhibition is due to domain immobilization and sets an upper limit for the concentration of this second messenger in the cell	Caulobacter vibrioides

Organism

Organism	UniProt	Comment	Textmining
Caulobacter vibrioides	-	isoform PleD	-

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Release 2023.1 (January 2023)