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Literature summary for 1.13.12.24 extracted from

  • Deng, L.; Vysotski, E.S.; Markova, S.V.; Liu, Z.J.; Lee, J.; Rose, J.; Wang, B.C.
    All three Ca2+-binding loops of photoproteins bind calcium ions the crystal structures of calcium-loaded apo-aequorin and apo-obelin (2005), Protein Sci., 14, 663-675 .
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
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 Aequorea victoria
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 Obelia longissima

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Aequorea victoria
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 Obelia longissima

Organism

Organism UniProt Comment Textmining
Aequorea victoria P02592
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Obelia longissima Q27709
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-

Synonyms

Synonyms Comment Organism
obelin
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 Obelia longissima