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Originally published In Press as doi:10.1074/jbc.M002976200 on July 11, 2000

J. Biol. Chem., Vol. 275, Issue 39, 30082-30087, September 29, 2000
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Evidence for Major Structural Changes in the Manduca sexta Midgut V1 ATPase Due to Redox Modulation
A SMALL ANGLE X-RAY SCATTERING STUDY*

Gerhard GrüberDagger §, Dmitri I. Svergun||**, Jasminka Godovac-ZimmermannDagger Dagger , William R. Harvey§, Helmut WieczorekDagger , and Michel H. J. Koch||

From the Dagger  Universität Osnabrück, Fachbereich Biologie/Chemie, D-49069 Osnabrück, Germany, the § Whitney Laboratory, University of Florida, St. Augustine, Florida 32086, the || European Molecular Biology Laboratory, Hamburg Outstation, EMBL c/o DESY, D-22603 Hamburg, Germany, the ** Institute of Crystallography, Russian Academy of Sciences, 117333 Moscow, Russia, and Dagger Dagger  University College London, Centre for Molecular Medicine, London WC1E 6JJ, United Kingdom

The shape and overall dimensions of the oxidized and reduced form of the V1 ATPase from Manduca sexta were investigated by synchrotron radiation x-ray solution scattering. The radius of gyration of the oxidized and reduced complex differ noticeably, with dimensions of 6.20 ± 0.06 and 5.84 ± 0.06 nm, respectively, whereas the maximum dimensions remain constant at 22.0 ± 0.1 nm. Comparison of the low resolution shapes of both forms, determined ab initio, indicates that the main structural alteration occurs in the head piece, where the major subunits A and B are located, and at the bottom of the stalk. In conjunction with the solution scattering data, decreased susceptibility to tryptic digestion and tryptophan fluorescence of the reduced V1 molecule provide the first strong evidence for major structural changes in the V1 ATPase because of redox modulation.

* This work was supported by Deutsche Forschungsgemeinschaft Grant SFB 431 and Habilitandenstipendium Grant GR 1475/6-1, National Institutes of Health Grant A1 22444, International Association for the Promotion of Cooperation with Scientists from the Independent States of the Former Soviet Union Grant 96-1115 (to D. I. S. and M. H. J. K.), and European Union Biotechnology Program Grant BIO4-CT97-2143 (to D. I. S.).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.

To whom correspondence should be addressed: Universität Osnabrück, Fachbereich Biologie/Chemie, D-49069 Osnabrück, Germany. Tel.: 49-541-969-3504; Fax: 49-541-969-3503; E-mail: grueber@ biologie.uni-osnabrueck.de.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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