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2bv8
From Proteopedia
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THE CRYSTAL STRUCTURE OF PHYCOCYANIN FROM GRACILARIA CHILENSIS.
Overview
Phycocyanin is a phycobiliprotein involved in light harvesting and, conduction of light to the reaction centers in cyanobacteria and red, algae. The structure of C-phycocyanin from Gracilaria chilensis was solved, by X-ray crystallography at 2.0 A resolution in space group P2(1). An, interaction model between two PC heterohexamers was built, followed by, molecular dynamic refinement. The best model showed an inter-hexamer, rotation of 23 degrees . The coordinates of a PC heterohexamer, (alphabeta)(6) and of the PC-PC complex were used to perform energy, transfer calculations between chromophores pairs using the fluorescence, resonance energy transfer approach (FRET). Two main intra PC, ((I)beta(3)(82)-->(I)alpha(1)(84)-->(I)alpha(5)(84)-->(I)beta(6)(82) and, (I)beta(3)(153)-->(I)beta(5)(153)) and two main inter PC, ((I)beta(6)(82)-->(II)beta(3)(82) and (I)beta(5)(153)-->(II)beta(3)(153)), pathways were proposed based on the values of the energy transfer, constants calculated for all the chromophore pairs in the hexamer and in, the complex.
About this Structure
2BV8 is a Protein complex structure of sequences from Gracilaria chilensis with and as ligands. Full crystallographic information is available from OCA.
Reference
The structure at 2 A resolution of Phycocyanin from Gracilaria chilensis and the energy transfer network in a PC-PC complex., Contreras-Martel C, Matamala A, Bruna C, Poo-Caamano G, Almonacid D, Figueroa M, Martinez-Oyanedel J, Bunster M, Biophys Chem. 2007 Feb;125(2-3):388-96. Epub 2006 Nov 10. PMID:17118524
Page seeded by OCA on Tue Jan 29 18:31:18 2008
