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1b8d

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{{Structure
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|LIGAND= <scene name='pdbligand=MEN:N-METHYL+ASPARAGINE'>MEN</scene>, <scene name='pdbligand=PEB:PHYCOERYTHROBILIN'>PEB</scene>, <scene name='pdbligand=PUB:PHYCOUROBILIN'>PUB</scene>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene>
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{{STRUCTURE_1b8d| PDB=1b8d | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b8d OCA], [http://www.ebi.ac.uk/pdbsum/1b8d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b8d RCSB]</span>
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'''CRYSTAL STRUCTURE OF A PHYCOUROBILIN-CONTAINING PHYCOERYTHRIN'''
'''CRYSTAL STRUCTURE OF A PHYCOUROBILIN-CONTAINING PHYCOERYTHRIN'''
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[[Category: Welte, W.]]
[[Category: Welte, W.]]
[[Category: Wrench, P M.]]
[[Category: Wrench, P M.]]
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[[Category: light-harvesting complex]]
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[[Category: Light-harvesting complex]]
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[[Category: phycobiliprotein]]
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[[Category: Phycobiliprotein]]
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[[Category: red algae]]
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[[Category: Red algae]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:11:53 2008''
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Revision as of 08:11, 2 May 2008

Template:STRUCTURE 1b8d

CRYSTAL STRUCTURE OF A PHYCOUROBILIN-CONTAINING PHYCOERYTHRIN


Overview

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.

About this Structure

1B8D is a Protein complex structure of sequences from Griffithsia monilis. Full crystallographic information is available from OCA.

Reference

Crystal structure of a phycourobilin-containing phycoerythrin at 1.90-A resolution., Ritter S, Hiller RG, Wrench PM, Welte W, Diederichs K, J Struct Biol. 1999 Jun 15;126(2):86-97. PMID:10388620 Page seeded by OCA on Fri May 2 11:11:53 2008

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