3D-Structure-Function of Light-harvesting Protein of Algae and the Transmission of Light Energy

    Under the support of the Key Program project of NSFC, CAS Member Liang Dongcai and colleagues of CAS Institute of Biophysics has studied the mechanism of light transfer in the light harvesting system of photosynthesis organisms. Through many years of efforts, they have successively finished the 3d-structure of R-Phycoerythrin in 2.8Å and 1.9Å resolution (J.Mol.Biol. (1996) 262,721-731; Proteins (1999) 34:224-231), R-Phycoerythrin in 2.4Å trdoluyion (Biophysical Journal (2001)) and Allophycocyanin in 2.2Å resolution (Acta Cryst. (1998) D54, 662-664; J.Biol.Chem. (1999) 274, 16945-16952) research, and they have given detailed studies on their functions They have brought forward the model of energy transferring within the Phycoerythrin and the possible energy transfer route between Phycoerythrin and near phycocyanin. They discovered that the function unit of Allophycocyanin is "loose hexamer", but is not the world commonlyecognized trimer. Through systematic studies, Prof. Liang and his colleagues developed the model of the energy transfer route within phycobillisome. This has established an important structural basis for elucidating the mechanism of energy transferring in the light harvesting system in algae.

    Sketch map of Ca atom of R-Phycoerythrin hexamer and pigment molecular in 1.9Å resolution, indicated by three independent parts in red, green and blue by axe-connection three times. The oxygen atom of pigment molecules is in red, carbon atom in yellow and nitrogen atom in blue.


    Molecule stack map of R-phycocyanin in crystal cells. The yellow and blue color indicate two different tightly stacked trimer (αβ)3 of R-phycocyanin, compared with other Biliproteins in crystal cells, and its cumuli method is quite typical.

    Sketch map of the route of energy transfer within R-Phycoerythrin. The four phycoerythrobilins connecting α84, β84, α140a and cysteine inβ155 position are in green color, the simultaneity connected pyhcourobilin with cysteine inβ50 and β61 cysteine is in pink.


   
Sketch map of ribbon of αsub-unit, βsub-unit of Allophycocyanin (left) and trimer (right). αsub-unit is indicated in green and βsub-unit in blue. The oxygen atom of pigment molecular is indicated in red balls, carbon atom in yellow balls and nitrogen atom in blue balls.