1lia
From Proteopedia
(New page: 200px<br /><applet load="1lia" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lia, resolution 2.8Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1lia.gif|left|200px]]<br /><applet load="1lia" size=" | + | [[Image:1lia.gif|left|200px]]<br /><applet load="1lia" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lia, resolution 2.8Å" /> | caption="1lia, resolution 2.8Å" /> | ||
'''CRYSTAL STRUCTURE OF R-PHYCOERYTHRIN FROM POLYSIPHONIA AT 2.8 A RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF R-PHYCOERYTHRIN FROM POLYSIPHONIA AT 2.8 A RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of R-phycoerythrin (R-PE) from Polysiphonia urceolata was | + | 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== | ==About this Structure== | ||
| - | 1LIA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Polysiphonia_urceolata Polysiphonia urceolata] with CYC and PUB as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1LIA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Polysiphonia_urceolata Polysiphonia urceolata] with <scene name='pdbligand=CYC:'>CYC</scene> and <scene name='pdbligand=PUB:'>PUB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LIA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Polysiphonia urceolata]] | [[Category: Polysiphonia urceolata]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Chang, W | + | [[Category: Chang, W R.]] |
[[Category: Jiang, T.]] | [[Category: Jiang, T.]] | ||
| - | [[Category: Liang, D | + | [[Category: Liang, D C.]] |
[[Category: CYC]] | [[Category: CYC]] | ||
[[Category: PUB]] | [[Category: PUB]] | ||
[[Category: light harvesting protein]] | [[Category: light harvesting protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:14 2008'' |
Revision as of 11:45, 21 February 2008
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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 with and as ligands. 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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