1lia: Difference between revisions
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'''CRYSTAL STRUCTURE OF R-PHYCOERYTHRIN FROM POLYSIPHONIA AT 2.8 A RESOLUTION''' | {{Structure | ||
|PDB= 1lia |SIZE=350|CAPTION= <scene name='initialview01'>1lia</scene>, resolution 2.8Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</scene> and <scene name='pdbligand=PUB:PHYCOUROBILIN'>PUB</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF R-PHYCOERYTHRIN FROM POLYSIPHONIA AT 2.8 A RESOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1LIA is a [ | 1LIA is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Polysiphonia_urceolata Polysiphonia urceolata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LIA OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8876649 8876649] | ||
[[Category: Polysiphonia urceolata]] | [[Category: Polysiphonia urceolata]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: light harvesting protein]] | [[Category: light harvesting protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:31:10 2008'' | ||
Revision as of 10:31, 20 March 2008
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| 1lia, resolution 2.8Å | |||||||||||||
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| Ligands: | CYC and PUB | ||||||||||||
| 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
Page seeded by OCA on Thu Mar 20 12:31:10 2008
