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Science 27 January 1995:
Vol. 267. no. 5197, pp. 512 - 514
DOI: 10.1126/science.7824948

Articles

Science, Vol 267, Issue 5197, 512-514
Copyright © 1995 by American Association for the Advancement of Science


articles

Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution

T Schirmer, TA Keller, YF Wang, and JP Rosenbusch

Department of Structural Biology, University of Basel, Switzerland.

Trimeric maltoporin (LamB protein) facilitates the diffusion of maltodextrins across the outer membrane of Gram-negative bacteria. The crystal structure of maltoporin from Escherichia coli, determined to a resolution of 3.1 angstroms, reveals an 18-stranded, antiparallel beta-barrel that forms the framework of the channel. Three inwardly folded loops contribute to a constriction about halfway through the channel. Six contingent aromatic residues line the channel and form a path from the vestibule to the periplasmic outlet. Soaking of a crystal with maltotriose revealed binding of the sugar to this hydrophobic track across the constriction, which suggests that maltose and linear oligosaccharides may be translocated across the membrane by guided diffusion along this path.


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