Rhodopsin-transducin heteropentamer : three-dimensional structure and biochemical characterization

Jastrzebska, B. and Ringler, P. and Lodowski, D. T. and Moiseenkova-Bell, V. and Golczak, M. and Muller, S. A. and Palczewski, K. and Engel, A.. (2011) Rhodopsin-transducin heteropentamer : three-dimensional structure and biochemical characterization. Journal of structural biology, Vol. 176, H. 3. pp. 387-394.

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Official URL: http://edoc.unibas.ch/dok/A6002469

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The process of vision is initiated when the G protein-coupled receptor, rhodopsin (Rho), absorbs a photon and transitions to its activated Rho( *) form. Rho( *) binds the heterotrimeric G protein, transducin (G(t)) inducing GDP to GTP exchange and G(t) dissociation. Using nucleotide depletion and affinity chromatography, we trapped and purified the resulting nucleotide-free Rho( *).G(t) complex. Quantitative SDS-PAGE suggested a 2:1 molar ratio of Rho( *) to G(t) in the complex and its mass determined by scanning transmission electron microscopy was 221+/-12kDa. A 21.6A structure was calculated from projections of negatively stained Rho( *).G(t) complexes. The molecular envelope thus determined accommodated two Rho molecules together with one G(t) heterotrimer, corroborating the heteropentameric structure of the Rho( *).G(t) complex.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel)
UniBasel Contributors:Engel, Andreas H
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:11 Oct 2012 15:31
Deposited On:11 Oct 2012 15:15

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