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

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


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RITTER, 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. 126(2), pp. 86-97. ISSN 1047-8477

@article{Ritter1999Cryst-6862, title={Crystal Structure of a Phycourobilin-Containing Phycoerythrin at 1.90-Å Resolution}, year={1999}, doi={10.1006/jsbi.1999.4106}, 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} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/6862"> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/6862"/> <dc:contributor>Wrench, Pamela M.</dc:contributor> <dc:contributor>Hiller, Roger G.</dc:contributor> <dc:contributor>Welte, Wolfram</dc:contributor> <dc:format>application/pdf</dc:format> <dc:contributor>Diederichs, Kay</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:29:44Z</dcterms:available> <dcterms:bibliographicCitation>First publ. in: Journal of Structural Biology 126 (1999), pp. 86-97</dcterms:bibliographicCitation> <dc:creator>Diederichs, Kay</dc:creator> <dcterms:issued>1999</dcterms:issued> <dc:language>eng</dc:language> <dc:contributor>Ritter, Stephan</dc:contributor> <dc:rights>deposit-license</dc:rights> <dc:creator>Wrench, Pamela M.</dc:creator> <dcterms:title>Crystal Structure of a Phycourobilin-Containing Phycoerythrin at 1.90-Å Resolution</dcterms:title> <dc:creator>Hiller, Roger G.</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:29:44Z</dc:date> <dc:creator>Welte, Wolfram</dc:creator> <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> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dc:creator>Ritter, Stephan</dc:creator> </rdf:Description> </rdf:RDF>

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