Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution

Athina Zouni, Horst-Tobias Witt, Jan Kern, Petra Fromme, Norbert Krauss, Wolfram Saenger () and Peter Orth
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Athina Zouni: Max-Volmer-Institut für Biophysikalische Chemie und Biochemie, Technische Universität Berlin
Horst-Tobias Witt: Max-Volmer-Institut für Biophysikalische Chemie und Biochemie, Technische Universität Berlin
Jan Kern: Max-Volmer-Institut für Biophysikalische Chemie und Biochemie, Technische Universität Berlin
Petra Fromme: Max-Volmer-Institut für Biophysikalische Chemie und Biochemie, Technische Universität Berlin
Norbert Krauss: Institut für Chemie, Kristallographie, Freie Universität Berlin
Wolfram Saenger: Institut für Chemie, Kristallographie, Freie Universität Berlin
Peter Orth: Institut für Chemie, Kristallographie, Freie Universität Berlin

Nature, 2001, vol. 409, issue 6821, 739-743

Abstract: Abstract Oxygenic photosynthesis is the principal energy converter on earth. It is driven by photosystems I and II, two large protein–cofactor complexes located in the thylakoid membrane and acting in series. In photosystem II, water is oxidized; this event provides the overall process with the necessary electrons and protons, and the atmosphere with oxygen. To date, structural information on the architecture of the complex has been provided by electron microscopy of intact, active photosystem II at 15–30 Å resolution1, and by electron crystallography on two-dimensional crystals of D1-D2-CP47 photosystem II fragments without water oxidizing activity at 8 Å resolution2. Here we describe the X-ray structure of photosystem II on the basis of crystals fully active in water oxidation3. The structure shows how protein subunits and cofactors are spatially organized. The larger subunits are assigned and the locations and orientations of the cofactors are defined. We also provide new information on the position, size and shape of the manganese cluster, which catalyzes water oxidation.

Date: 2001
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DOI: 10.1038/35055589

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