The 3.7 projection map of the glycerol facilitator GlpF: A variant of the aquaporin tetramer

Braun, Thomas and Philippsen, Ansgar and Wirtz, Sabine and Borgnia, Mario J. and Agre, Peter and Kühlbrandt, Werner and Engel, Andreas and Stahlberg, Henning. (2000) The 3.7 projection map of the glycerol facilitator GlpF: A variant of the aquaporin tetramer. EMBO Reports, 1 (2). pp. 183-189.

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GlpF, the glycerol facilitator protein of Escherichia coli, is an archetypal member of the aquaporin superfamily. To assess its structure, recombinant histidine-tagged protein was overexpressed, solubilized in octylglucoside and purified to homogeneity. Negative stain electron microscopy of solubilized GlpF protein revealed a tetrameric structure of similar to 80 Angstrom side length. Scanning transmission electron microscopy yielded a mass of 170 kDa, corroborating the tetrameric nature of GlpF. Reconstitution of GlpF in the presence of lipids produced highly ordered two-dimensional crystals, which diffracted electrons to 3.6 Angstrom resolution. Cryoelectron microscopy provided a 3.7 Angstrom projection map exhibiting a unit cell comprised of two tetramers. In projection, GlpF is similar to AQP1, the erythrocyte water channel. However, the major density minimum within each monomer is distinctly larger in GlpF than in AQP1.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Braun)
05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Stahlberg)
UniBasel Contributors:Braun, Thomas
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Nature Publishing Group
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:31 May 2021 10:11
Deposited On:31 May 2021 10:11

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