Abstract
Here we present cryoelectron crystallographic analysis of an isolated dimeric oxygen-evolving complex of photosystem II (at a resolution of ~0.9 nm), revealing that the D1–D2 reaction center (RC) proteins are centrally located between the chlorophyll-binding proteins, CP43 and CP47. This conclusion supports the hypothesis that photosystems I and II have similar structural features and share a common evolutionary origin. Additional density connecting the two halves of the dimer, which was not observed in a recently described CP47–RC complex that did not include CP43, may be attributed to the small subunits that are involved in regulating secondary electron transfer, such as PsbH. These subunits are possibly also required for stabilization of the dimeric photosystem II complex. This complex, containing at least 29 transmembrane helices in its asymmetric unit, represents one of the largest membrane protein complexes studied at this resolution.
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Acknowledgements
We thank the BBSRC for financial support, B. Gowen, S. Chen and H. Saibil for help with electron microscopy and sample preparation, M. van Heel for the use of a densitometer and computing facilities and J. Nield for preparing Fig. 1. We also thank W. Kühlbrandt and P. Fromme for valuable discussions on this work.
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Hankamer, B., Morris, E. & Barber, J. Revealing the structure of the oxygen-evolving core dimer of photosystem II by cryoelectron crystallography. Nat Struct Mol Biol 6, 560–564 (1999). https://doi.org/10.1038/9341
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DOI: https://doi.org/10.1038/9341
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