Goc, A. and Chami, M. and Lodowski, D. T. and Bosshart, P. and Moiseenkova-Bell, V. and Baehr, W. and Engel, A. and Palczewski, K.. (2010) Structural characterization of the rod cGMP phosphodiesterase 6. Journal of molecular biology, Vol. 401, H. 3. pp. 363-373.
Full text not available from this repository.
Official URL: http://edoc.unibas.ch/dok/A6002465
Downloads: Statistics Overview
Abstract
Rod cGMP phosphodiesterase 6 (PDE6) is a key enzyme of the phototransduction cascade, consisting of PDE6alpha, PDE6beta, and two regulatory PDE6gamma subunits. PDE6 is membrane associated through isoprenyl membrane anchors attached to the C-termini of PDE6alpha and PDE6beta and can form a complex with prenyl-binding protein delta (PrBP/delta), an isoprenyl-binding protein that is highly expressed in photoreceptors. The stoichiometry of PDE6-PrBP/delta binding and the mechanism by which the PDE6-PrBP/delta complex assembles have not been fully characterized, and the location of regulatory PDE6gamma subunits within the protein assembly has not been elucidated. To clarify these questions, we have developed a rapid purification method for PDE6-PrBP/delta from bovine rod outer segments utilizing recombinant PrBP/delta. Transmission electron microscopy of negatively stained samples revealed the location of PrBP/delta and, thus, where the carboxyl-termini of PDE6alpha and PDE6beta must be located. The three-dimensional structure of the PDE6alphabetagamma complex was determined up to 18 A resolution from single-particle projections and was interpreted by model building to identify the probable location of isoprenylation, PDE6gamma subunits, and catalytic sites.
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 |
Publisher: | Elsevier |
ISSN: | 0022-2836 |
Note: | Publication type according to Uni Basel Research Database: Journal article |
Identification Number: | |
Last Modified: | 14 Sep 2012 07:22 |
Deposited On: | 14 Sep 2012 07:15 |
Repository Staff Only: item control page