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The c15 ring of the Spirulina platensis F-ATP synthase: F1/F0 symmetry mismatch is not obligatory

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Meier,  Thomas
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Vonck,  Janet       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Pogoryelov, D., Yu, J., Meier, T., Vonck, J., Dimroth, P., & Muller, D. J. (2005). The c15 ring of the Spirulina platensis F-ATP synthase: F1/F0 symmetry mismatch is not obligatory. EMBO Reports, 6(11), 1040-1044. doi:10.1038/sj.embor.7400517.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-DA26-6
Abstract
he oligomeric c ring of the F-ATP synthase from the alkaliphilic cyanobacterium Spirulina platensis was isolated and characterized. Mass spectroscopy analysis indicated a mass of 8,210 Da, reflecting that of a c monomer. The mass increased by 206 Da after treatment with the c-subunit-specific inhibitor dicyclohexylcarbodiimide (DCCD), which indicated modification of the ion-binding carboxylate by DCCD. Atomic force microscopy topographs of c rings from S. platensis showed 15 symmetrically assembled subunits. The c15-mer reported here is the largest c ring that is isolated and does not show the classical c-ring mismatch to the three-fold symmetry of the F1 domain.