1lia
From Proteopedia
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|PDB= 1lia |SIZE=350|CAPTION= <scene name='initialview01'>1lia</scene>, resolution 2.8Å | |PDB= 1lia |SIZE=350|CAPTION= <scene name='initialview01'>1lia</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</scene> | + | |LIGAND= <scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</scene>, <scene name='pdbligand=PUB:PHYCOUROBILIN'>PUB</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lia OCA], [http://www.ebi.ac.uk/pdbsum/1lia PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lia RCSB]</span> | ||
}} | }} | ||
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[[Category: Jiang, T.]] | [[Category: Jiang, T.]] | ||
[[Category: Liang, D C.]] | [[Category: Liang, D C.]] | ||
| - | [[Category: CYC]] | ||
| - | [[Category: PUB]] | ||
[[Category: light harvesting protein]] | [[Category: light harvesting protein]] | ||
| - | ''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 22:03:10 2008'' |
Revision as of 19:03, 30 March 2008
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| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF R-PHYCOERYTHRIN FROM POLYSIPHONIA AT 2.8 A RESOLUTION
Overview
The structure of R-phycoerythrin (R-PE) from Polysiphonia urceolata was determined at 2.8 A resolution. The crystals belong to space group R3 with unit cell dimensions of a = b = 189.8 A, c = 60.1 A. The subunit composition of R-PE is (alpha 2 beta 2)3 gamma. The three-dimensional structure of R-PE was solved by the multiple isomorphous replacement method. After several cycles of model building and refinement, the crystallographic R-factor of the final model is 18.0% with data from 10.0 to 2.8 A resolution. The four phycoerythrobilin chromophores alpha 84, alpha 140a, beta 84 and beta 155 in an (alpha beta) unit are each covalently bound to a cysteine residue through ring A. The phycourobilin chromophore is bound to cysteine beta 50 by ring A and bound to cysteine beta 61 by ring D. The ring A and ring D of phycourobilin deviate from the conjugate plane formed by ring B and ring C and the four rings form a boat-shaped structure. R-PE contains a 34 kDa gamma subunit that is assumed to lie in the central channel of the molecular disc (alpha 2 beta 2)3. The energy transfer and relationship between cysteine residues and chromophores are discussed.
About this Structure
1LIA is a Protein complex structure of sequences from Polysiphonia urceolata. Full crystallographic information is available from OCA.
Reference
Crystal structure of R-phycoerythrin from Polysiphonia urceolata at 2.8 A resolution., Chang WR, Jiang T, Wan ZL, Zhang JP, Yang ZX, Liang DC, J Mol Biol. 1996 Oct 11;262(5):721-31. PMID:8876649
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