Abstract:
: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 approximately 80 A 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 A resolution. Cryoelectron microscopy provided a 3.7 A 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.
journal_name
EMBO Repjournal_title
EMBO reportsauthors
Braun T,Philippsen A,Wirtz S,Borgnia MJ,Agre P,Kühlbrandt W,Engel A,Stahlberg Hdoi
10.1093/embo-reports/kvd022keywords:
subject
Has Abstractpub_date
2000-08-01 00:00:00pages
183-9issue
2eissn
1469-221Xissn
1469-3178pii
embor615journal_volume
1pub_type
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