Literature summary for 2.7.7.65 extracted from

Tarnawski, M.; Barends, T.R.; Schlichting, I.
Structural analysis of an oxygen-regulated diguanylate cyclase (2015), Acta Crystallogr. Sect. D, 71, 2158-2177.

Crystallization (Commentary)

Crystallization (Comment)	Organism
structural characterization of the oxygen-sensing globin domain, the middle domain and the catalytic GGDEF omain in apo and substrate-bound forms. The structural changes between the iron(III) and iron(II) forms of the sensor globin domain suggest a mechanism for oxygen-dependent regulation. Enzyme forms a constitutive dimer and in this form its enzymatic activity is regulated by oxygen binding. The middle domain of DosC connects the sensory and effector modules and is likely to be both essential for and directly involved in the intramolecular signal transduction in DosC	Escherichia coli

Crystallization (Comment)

Organism

structural characterization of the oxygen-sensing globin domain, the middle domain and the catalytic GGDEF omain in apo and substrate-bound forms. The structural changes between the iron(III) and iron(II) forms of the sensor globin domain suggest a mechanism for oxygen-dependent regulation. Enzyme forms a constitutive dimer and in this form its enzymatic activity is regulated by oxygen binding. The middle domain of DosC connects the sensory and effector modules and is likely to be both essential for and directly involved in the intramolecular signal transduction in DosC

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AA89	-	-

Synonyms

Synonyms	Comment	Organism
DosC	-	Escherichia coli

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Release 2023.1 (January 2023)