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Originally published In Press as doi:10.1074/jbc.M008015200 on October 13, 2000

J. Biol. Chem., Vol. 276, Issue 2, 1345-1352, January 12, 2001
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The Structure of the Chloroplast F1-ATPase at 3.2 Å Resolution*

Georg GrothDagger § and Ehmke Pohl

From the Dagger  Heinrich-Heine-Universität, Biochemie der Pflanzen, Universitätsstrasse 1, D-40225 Düsseldorf, Germany and  EMBL Hamburg, Notkestrasse 85, D-22603 Hamburg, Germany

The structure of the F1-ATPase from spinach chloroplasts was determined to 3.2 Å resolution by molecular replacement based on the homologous structure of the bovine mitochondrial enzyme. The crystallized complex contains four different subunits in a stoichiometry of alpha 3beta 3gamma epsilon . Subunit delta  was removed before crystallization to improve the diffraction of the crystals. The overall structure of the noncatalytic alpha -subunits and the catalytic beta -subunits is highly similar to those of the mitochondrial and thermophilic subunits. However, in the crystal structure of the chloroplast enzyme, all alpha - and beta -subunits adopt a closed conformation and appear to contain no bound adenine nucleotides. The superimposed crystallographic symmetry in the space group R32 impaired an exact tracing of the gamma - and epsilon -subunits in the complex. However, clear electron density was present at the core of the alpha 3beta 3-subcomplex, which probably represents the C-terminal domain of the gamma -subunit. The structure of the spinach chloroplast F1 has a potential binding site for the phytotoxin, tentoxin, at the alpha beta -interface near beta Asp83 and an insertion from beta Gly56-Asn60 in the N-terminal beta -barrel domain probably increases the thermal stability of the complex. The structure probably represents an inactive latent state of the ATPase, which is unique to chloroplast and cyanobacterial enzymes.

* This work was supported by Deutsche Forschungsgemeinschaft Grant Gr1616/4-1 and by funds from the Bennigsen-Foerder-Preis of Nordrhein-Westfalen (to G. G.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and the structure factors (code 1FX0) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

This article is dedicated to Wolfgang Junge (Osnabrück) on the occasion of his 60th birthday.

§ To whom correspondence should be addressed. Tel.: 49-211-8112822; Fax: 49-211-8113706; E-mail: georg.groth@uni- duesseldorf.de.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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