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Title
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The molecular structure of green fluorescent protein.
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Authors
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F.Yang,
L.G.Moss,
G.N.Phillips.
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Ref.
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Nat Biotechnol, 1996,
14,
1246-1251.
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PubMed id
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Abstract
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The crystal structure of recombinant wild-type green fluorescent protein (GFP)
has been solved to a resolution of 1.9 A by multiwavelength anomalous dispersion
phasing methods. The protein is in the shape of a cylinder, comprising 11
strands of beta-sheet with an alpha-helix inside and short helical segments on
the ends of the cylinder. This motif, with beta-structure on the outside and
alpha-helix on the inside, represents a new protein fold, which we have named
the beta-can. Two protomers pack closely together to form a dimer in the
crystal. The fluorophores are protected inside the cylinders, and their
structures are consistent with the formation of aromatic systems made up of
Tyr66 with reduction of its C alpha-C beta bond coupled with cyclization of the
neighboring glycine and serine residues. The environment inside the cylinder
explains the effects of many existing mutants of GFP and suggests specific side
chains that could be modified to change the spectral properties of GFP.
Furthermore, the identification of the dimer contacts may allow mutagenic
control of the state of assembly of the protein.
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