Literature summary for 4.6.1.1 extracted from

Lindner, R.; Hartmann, E.; Tarnawski, M.; Winkler, A.; Frey, D.; Reinstein, J.; Meinhart, A.; Schlichting, I.
Photoactivation mechanism of a bacterial light-regulated adenylyl cyclase (2017), J. Mol. Biol., 429, 1336-1351 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Beggiatoa sp. PS

Crystallization (Commentary)

Crystallization (Comment)	Organism
dark state crystal structure and structures of illuminated enzyme	Beggiatoa sp. PS

Organism

Organism	UniProt	Comment	Textmining
Beggiatoa sp. PS	A7BT71	beta-subunit	-

Synonyms

Synonyms	Comment	Organism
BGP_1043	-	Beggiatoa sp. PS

General Information

General Information	Comment	Organism
physiological function	the enzyme contains a BLUF (blue light sensor using flavin) photoreceptor domain that senses blue light using a flavin chromophore, linked to an adenylate cyclase domain. A direct pathway links the conformation of the active site Tyr and Gln to a prominent conserved kink in beta4BLUF and from there to the C-terminal BLUF capping helix. The beta4AC-beta5AC tongue is a central toggle that interacts with a regulatory domain to adjust adenylate cyclase opening and to prepare the active site for catalysis	Beggiatoa sp. PS

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Release 2023.1 (January 2023)