Maltoporins (or LamB porins) are a family of outer membrane proteins. Maltoporin forms a trimeric structure which facilitates the diffusion of maltodextrins across the outer membrane of Gram-negative bacteria. The membrane channel is formed by an antiparallel beta-barrel. Maltoporin is a trimeric channel on the bacterial outer membrane. Most pores used for diffusion contain only 16 antiparallel strands, but Maltoporin has 18. The structure of Maltoporin contains long loops and short turns. The long loops are in contact with the cell exterior and the turns are in contact with the periplasm. This channel is involved in sugar transport. The sugar initially binds to the first greasy residue with van der Waals forces. The sugar continues through the channel by guided diffusion of the sugar along the greasy residues which form a "slide". Maltoporin's original name was LamB because it is a bacteriophage lambda receptor. This channel is specific because it has a binding site for maltosaccharides. The affinity of these maltosaccharides to the channel increases as the length of the chain increases.
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