Crystal Structure of a Phycourobilin-Containing Phycoerythrin at 1.90-Å Resolution

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1999
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Ritter, Stephan
Hiller, Roger G.
Wrench, Pamela M.
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The structure of R-phycoerythrin (R-PE) from the red alga Griffithsia monilis was solved at 1.90-Å 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 Å. The model consists of an (αβ)2 dimer with an internal noncrystallographic dyad and a fragment of the γ-polypeptide. The α-polypeptide (164 amino acid residues) has two covalently bound phycoerythrobilins at positions α82 and α139. The β-polypeptide (177 residues) has two phycoerythrobilins bound to residues β82 and β158 and one phycourobilin covalently attached to rings A and D at residues β50 and β61, respectively. The electron density of the g-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 γ-polypeptide are in close proximity to the phycoerythrobilins at position β82 of two symmetry-related β-polypeptides and are related by the same noncrystallographic dyad as the (αβ)2 dimer. Possible energy transfer pathways are discussed briefly.

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570 Biowissenschaften, Biologie
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light-harvesting complexes, red algae, phycobiliproteins, protein structure, molecular replacement
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ISO 690RITTER, Stephan, Roger G. HILLER, Pamela M. WRENCH, Wolfram WELTE, Kay DIEDERICHS, 1999. Crystal Structure of a Phycourobilin-Containing Phycoerythrin at 1.90-Å Resolution. In: Journal of Structural Biology. 1999, 126(2), pp. 86-97. ISSN 1047-8477. Available under: doi: 10.1006/jsbi.1999.4106
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@article{Ritter1999Cryst-6862,
  year={1999},
  doi={10.1006/jsbi.1999.4106},
  title={Crystal Structure of a Phycourobilin-Containing Phycoerythrin at 1.90-Å Resolution},
  number={2},
  volume={126},
  issn={1047-8477},
  journal={Journal of Structural Biology},
  pages={86--97},
  author={Ritter, Stephan and Hiller, Roger G. and Wrench, Pamela M. and Welte, Wolfram and Diederichs, Kay}
}
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    <dcterms:abstract xml:lang="eng">The structure of R-phycoerythrin (R-PE) from the red alga Griffithsia monilis was solved at 1.90-Å 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 Å. The model consists of an (αβ)2 dimer with an internal noncrystallographic dyad and a fragment of the γ-polypeptide. The α-polypeptide (164 amino acid residues) has two covalently bound phycoerythrobilins at positions α82 and α139. The β-polypeptide (177 residues) has two phycoerythrobilins bound to residues β82 and β158 and one phycourobilin covalently attached to rings A and D at residues β50 and β61, respectively. The electron density of the g-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 γ-polypeptide are in close proximity to the phycoerythrobilins at position β82 of two symmetry-related β-polypeptides and are related by the same noncrystallographic dyad as the (αβ)2 dimer. Possible energy transfer pathways are discussed briefly.</dcterms:abstract>
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