In vivo and in vitro studies of major surface loop deletion mutants of the Escherichia coli K-12 maltoporin: contribution to maltose and maltooligosaccharide transport and binding.

@article{Andersen1999InVA,
  title={In vivo and in vitro studies of major surface loop deletion mutants of the Escherichia coli K-12 maltoporin: contribution to maltose and maltooligosaccharide transport and binding.},
  author={Christian Andersen and Christoph Bachmeyer and H T{\"a}uber and Roland Benz and Jiyi Wang and Val{\'e}rie Michel and Sarah M Newton and M. Hofnung and Alain Charbit},
  journal={Molecular microbiology},
  year={1999},
  volume={32 4},
  pages={851-67}
}
The trimeric protein LamB of Escherichia coli K-12 (maltoporin) specifically facilitates the diffusion of maltose and maltooligosaccharides through the outer membrane. Each monomer consists of an 18-stranded antiparallel beta-barrel with nine surface loops (L1 to L9). The effects on transport and binding of the deletion of some of the surface loops or of combinations of several of them were studied in vivo and in vitro. In vivo, single-, DeltaL4, DeltaL5, DeltaL6, and double-loop deletions… CONTINUE READING