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PDBsum entry 1b8d
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Photosynthesis
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PDB id
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1b8d
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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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Crystal structure of a phycourobilin-Containing phycoerythrin at 1.90-A resolution.
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Authors
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S.Ritter,
R.G.Hiller,
P.M.Wrench,
W.Welte,
K.Diederichs.
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Ref.
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J Struct Biol, 1999,
126,
86-97.
[DOI no: ]
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PubMed id
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Abstract
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The structure of R-phycoerythrin (R-PE) from the red alga Griffithsia monilis
was solved at 1.90-A resolution by molecular replacement, using the atomic
coordinates of cyanobacterial phycocyanin from Fremyella diplosiphon as a model.
The crystallographic R factor for the final model is 17.5% (Rfree 22.7%) for
reflections in the range 100-1.90 A. The model consists of an (alphabeta)2 dimer
with an internal noncrystallographic dyad and a fragment of the
gamma-polypeptide. The alpha-polypeptide (164 amino acid residues) has two
covalently bound phycoerythrobilins at positions alpha82 and alpha139. The
beta-polypeptide (177 residues) has two phycoerythrobilins bound to residues
beta82 and beta158 and one phycourobilin covalently attached to rings A and D at
residues beta50 and beta61, respectively. The electron density of the
gamma-polypeptide is mostly averaged out by threefold crystallographic symmetry,
but a dipeptide (Gly-Tyr) and one single Tyr could be modeled. These two
tyrosine residues of the gamma-polypeptide are in close proximity to the
phycoerythrobilins at position beta82 of two symmetry-related beta-polypeptides
and are related by the same noncrystallographic dyad as the (alphabeta)2 dimer.
Possible energy transfer pathways are discussed briefly.
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