Literature summary for 1.13.12.24 extracted from

Head, J.F.; Inouye, S.; Teranishi, K.; Shimomura, O.
The crystal structure of the photoprotein aequorin at 2.3 A resolution (2000), Nature, 405, 372-376 .

Search for more literature for 1.13.12.24

Cloned(Commentary)

Cloned (Comment)	Organism
-	Aequorea victoria

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 2.3 A resolution. Aequorin is a globular molecule containing a hydrophobic core cavity that accommodates the ligand coelenterazine-2-hydroperoxide	Aequorea victoria

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	when calcium binds at either or both EF hands I and IV the helices of these hands will change their relative orientations	Aequorea victoria

Organism

Organism	UniProt	Comment	Textmining
Aequorea victoria	P02592	-	-

General Information

General Information	Comment	Organism
physiological function	when calcium binds at either or both EF hands I and IV the helices of these hands will change their relative orientations. Displacement of the helices flanking the C-terminal loop would disrupt the hydrogen-bonding network of the loop, resulting in a relocation of the side chain of Tyr 184. This would disrupt the hydrogen bonds to His 169 and the peroxide. The peroxide would be free to attack the adjacent carbonylic C3 to initiate the light-emitting reaction. The C-terminal tail could become partly or completely uncoupled from the helices, opening up the ligand-binding site to permit the egress of one or both reaction products	Aequorea victoria

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)