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PDBsum entry 2hps
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Luminescent protein
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PDB id
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2hps
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References listed in PDB file
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Key reference
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Title
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Crystal structure of coelenterazine-Binding protein from renilla muelleri at 1.7 a: why it is not a calcium-Regulated photoprotein.
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Authors
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G.A.Stepanyuk,
Z.J.Liu,
S.S.Markova,
L.A.Frank,
J.Lee,
E.S.Vysotski,
B.C.Wang.
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Ref.
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Photochem Photobiol Sci, 2008,
7,
442-447.
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PubMed id
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Abstract
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Bioluminescence in the sea pansy Renilla involves two distinct proteins, a
Ca2+-triggered coelenterazine-binding protein (CBP), and Renilla luciferase. CBP
contains one tightly bound coelenterazine molecule, which becomes available for
reaction with luciferase and O2 only subsequent to Ca2+ binding. CBP belongs to
the EF-hand superfamily of Ca2+-binding proteins and contains three "EF-hand"
Ca2+-binding sites. The overall spatial structure of recombinant
selenomethionine-labeled CBP determined at 1.7 A, is found to approximate the
protein scaffold characteristic of the class of Ca2+-regulated photoproteins.
Photoproteins however, catalyze molecular oxygen addition to coelenterazine
producing a 2-hydroperoxycoelenterazine intermediate, which is stabilized within
the binding cavity in the absence of Ca2+. Addition of Ca2+ triggers the
bioluminescence reaction. However in CBP this first step of oxygen addition is
not allowed. The different amino acid environments and hydrogen bond
interactions within the binding cavity, are proposed to account for the
different properties of the two classes of proteins.
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