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PDBsum entry 2ddd
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Luminescent protein
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PDB id
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2ddd
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References listed in PDB file
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Key reference
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Title
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The e1 mechanism in photo-Induced beta-Elimination reactions for green-To-Red conversion of fluorescent proteins.
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Authors
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H.Tsutsui,
H.Shimizu,
H.Mizuno,
N.Nukina,
T.Furuta,
A.Miyawaki.
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Ref.
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Chem Biol, 2009,
16,
1140-1147.
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PubMed id
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Abstract
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KikGR is a fluorescent protein engineered to display green-to-red
photoconvertibility that is induced by irradiation with ultraviolet or violet
light. Similar to Kaede and EosFP, two naturally occurring photoconvertible
proteins, KikGR contains a His(62)-Tyr(63)-Gly(64) tripeptide sequence, which
forms a green chromophore that can be photoconverted to a red one via formal
beta-elimination and subsequent extension of a pi-conjugated system. Using a
crystallizable variant of KikGR, we determined the structures of both the green
and red state at 1.55 A resolution. The double bond between His(62)-C(alpha) and
His(62)-C(beta) in the red chromophore is in a cis configuration, indicating
that rotation along the His(62) C(alpha)-C(beta) bond occurs following cleavage
of the His(62) N(alpha)-C(alpha) bond. This structural rearrangement provides
evidence that the beta-elimination reaction governing the green-to-red
photoconversion of KikGR follows an E1 (elimination, unimolecular) mechanism.
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