The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Molecular design of PhoE porin and its functional consequences.

The three-dimensional structure of PhoE porin from Escherichia coli, negatively stained with uranyl acetate, has been determined by electron crystallographic techniques to a resolution of about 18 A. The structure shows that PhoE porin consists of trimeric stain-filled channels as the basic unit. The trimeric channels converge as they transverse the membrane but they do not merge. Our three-dimensional structure of PhoE porin indicates that there is a short, narrower segment of channel, which extends beyond the visible strain-filled portion of the channel. The map of glucose-embedded PhoE porin in projection normal to the membrane has also been determined to a resolution of 6.5 A. The projected map shows trimeric ring-like structures, which are presumably cylindrical domains of beta-sheet. At the 3-fold symmetry axis of the trimer, there is a low density region, which is suggested to be a site of lipopolysaccharide that is required for channel and bacteriophage receptor activities. The structural model of the PhoE monomer consists of a flattened cylinder with a large water-filled vestibule about 35 A long with an elliptically shaped opening that is 27 A along the major axis and 18 A along the minor axis. The vestibule has a narrower extension about 10 A long with an average diameter of about 10 A. The vestibule wall is formed by beta-sheet, which may have a large fraction of the beta-strands oriented normal to membrane. Our structural model provides a clue as to how the surface charges on the outer membrane may regulate the permeation of ionic solutes through the channel.[1]


WikiGenes - Universities