Phosphorylation Controls the Three-dimensional Structure of Plant Light Harvesting Complex II*

The most abundant chlorophyll-binding complex in plants is the intrinsic membrane protein light-harvest-ing complex II (LHC II). LHC II acts as a light-harvesting antenna and has an important role in the distribution of absorbed energy between the two photosystems of pho-tosynthesis. We used spectroscopic techniques to study a synthetic peptide with identical sequence to the LHC IIb N terminus found in pea, with and without the phos-phorylated Thr at the 5th amino acid residue, and to study both forms of the native full-length protein. Our results show that the N terminus of LHC II changes structure upon phosphorylation and that the structural change resembles that of rabbit glycogen phosphoryl-ase, one of the few phosphoproteins where both phos-phorylated and non-phosphorylated structures hav