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PDBsum entry 1el4
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Luminescent protein
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PDB id
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1el4
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of the ca2+-Regulated photoprotein obelin at 1.7 a resolution determined directly from its sulfur substructure.
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Authors
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Z.J.Liu,
E.S.Vysotski,
C.J.Chen,
J.P.Rose,
J.Lee,
B.C.Wang.
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Ref.
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Protein Sci, 2000,
9,
2085-2093.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of the photoprotein obelin (22.2 kDa) from Obelia
longissima has been determined and refined to 1.7 A resolution. Contrary to the
prediction of a peroxide, the noncovalently bound substrate, coelenterazine, has
only a single oxygen atom bound at the C2-position. The protein-coelenterazine
2-oxy complex observed in the crystals is photo-active because, in the presence
of calcium ion, bioluminescence emission within the crystal is observed. This
structure represents only the second de novo protein structure determined using
the anomalous scattering signal of the sulfur substructure in the crystal. The
method used here is theoretically different from that used for crambin in 1981
(4.72 kDa) and represents a significant advancement in protein crystal structure
determination.
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Secondary reference #1
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Title
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Preparation and preliminary study of crystals of the recombinant calcium-Regulated photoprotein obelin from the bioluminescent hydroid obelia longissima.
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Authors
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E.S.Vysotski,
Z.J.Liu,
J.Rose,
B.C.Wang,
J.Lee.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1999,
55,
1965-1966.
[DOI no: ]
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PubMed id
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Figure 1.
Figure 1 Crystal of the photoprotein obelin, grown from 1.4 M
sodium citrate. Approximate dimensions are 0.1 × 0.1 × 1.0 mm.
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The above figure is
reproduced from the cited reference
with permission from the IUCr
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