1.13.12.24: calcium-regulated photoprotein
This is an abbreviated version!
For detailed information about calcium-regulated photoprotein, go to the full flat file.
Word Map on EC 1.13.12.24
-
1.13.12.24
-
photoproteins
-
bioluminescence
-
aequorin
-
luminescence
-
obelia
-
longissima
-
coelenteramide
-
ctenophore
-
coelenterate
-
jellyfish
-
ef-hand
-
2-hydroperoxycoelenterazine
-
mnemiopsis
-
hydroid
-
clytin
-
hydromedusan
-
leidyi
-
synthesis
-
analysis
- 1.13.12.24
-
photoproteins
-
bioluminescence
- aequorin
-
luminescence
- obelia
- longissima
- coelenteramide
-
ctenophore
-
coelenterate
-
jellyfish
-
ef-hand
- 2-hydroperoxycoelenterazine
- mnemiopsis
- hydroid
- clytin
-
hydromedusan
- leidyi
- synthesis
- analysis
Reaction
Synonyms
aequorin, alcium-activated photoprotein, berovin, BFP-aq, blue fluorescent protein, Ca2+-binding photoprotein, Ca2+-regulated photoprotein, clytin, halistaurin, mitrocomin, mnemiopsin, mnemiopsin 1, mnemiopsin 2, mnemiopsin1, obelin, phialidin
ECTree
Advanced search results
Crystallization
Crystallization on EC 1.13.12.24 - calcium-regulated photoprotein
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
hanging drop vapor diffusion method at 20°C, crystal structures of the apoAequorin complexes with the chiral deaza-analogs (S)-daCTZ and (S)-HM-daCTZ are determined, suggesting that the hydroxy moiety at the C6-hydroxyphenyl group and the carbonyl moiety of the imidazopyrazinone ring in coelenterazine are essential to bind the apoAequorin molecule through hydrogen bonding
to 1.7 A resolution. A calcium ion is observed in each of the three EF-hand loops that have the canonical calcium-binding sequence, and each is coordinated in the characteristic pentagonal bipyramidal configuration. The calcium-loaded apo-protein retains the same compact scaffold and overall fold as the unreacted photoprotein containing the bound substrate, 2-hydroperoxycoelenterazine
to 2.3 A resolution. Aequorin is a globular molecule containing a hydrophobic core cavity that accommodates the ligand coelenterazine-2-hydroperoxide
recombinantly expressed in Escherichia coli with Hexa-His-tag tail at N-terminal
sitting drop vapor diffusion method, crystal structure of Cd2+-loaded apo-mnemiopsin1 at 2.15 A resolution. The structure reveals that mnemiopsin1 has a two-domain fold with four alpha-helices in each domain
to 1.7 A resolution. A calcium ion is observed in each of the three EF-hand loops that have the canonical calcium-binding sequence, and each is coordinated in the characteristic pentagonal bipyramidal configuration. The calcium-loaded apo-protein retains the same compact scaffold and overall fold as the unreacted photoprotein containing the bound substrate, 2-hydroperoxycoelenterazine and also the same as the Ca2+-discharged obelin bound with the product, coelenteramide