1b8d
From Proteopedia
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|PDB= 1b8d |SIZE=350|CAPTION= <scene name='initialview01'>1b8d</scene>, resolution 1.90Å | |PDB= 1b8d |SIZE=350|CAPTION= <scene name='initialview01'>1b8d</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PEB:PHYCOERYTHROBILIN'>PEB</scene> | + | |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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Welte, W.]] | [[Category: Welte, W.]] | ||
[[Category: Wrench, P M.]] | [[Category: Wrench, P M.]] | ||
| - | [[Category: PEB]] | ||
| - | [[Category: PUB]] | ||
[[Category: light-harvesting complex]] | [[Category: light-harvesting complex]] | ||
[[Category: phycobiliprotein]] | [[Category: phycobiliprotein]] | ||
[[Category: red algae]] | [[Category: red algae]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:55:49 2008'' |
Revision as of 15:55, 30 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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