
doi: 10.1042/bst20170299
pmid: 29487228
Plant photosystem I (PSI) is one of the most intricate membrane complexes in nature. It comprises two complexes, a reaction center and light-harvesting complex (LHC), which together form the PSI–LHC supercomplex. The crystal structure of plant PSI was solved with two distinct crystal forms. The first, crystallized at pH 6.5, exhibited P21 symmetry; the second, crystallized at pH 8.5, exhibited P212121 symmetry. The surfaces involved in binding plastocyanin and ferredoxin are identical in both forms. The crystal structure at 2.6 Å resolution revealed 16 subunits, 45 transmembrane helices, and 232 prosthetic groups, including 143 chlorophyll a, 13 chlorophyll b, 27 β-carotene, 7 lutein, 2 xanthophyll, 1 zeaxanthin, 20 monogalactosyl diglyceride, 7 phosphatidyl diglyceride, 5 digalactosyl diglyceride, 2 calcium ions, 2 phylloquinone, and 3 iron sulfur clusters. The model reveals detailed interactions, providing mechanisms for excitation energy transfer and its modulation in one of nature's most efficient photochemical machine.
Photosystem I Protein Complex, Protein Conformation, Plants, Crystallography, X-Ray, Protein Binding
Photosystem I Protein Complex, Protein Conformation, Plants, Crystallography, X-Ray, Protein Binding
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