1mal

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spinqualitylabelsall models 1mal, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURAL BASIS FOR SUGAR TRANSLOCATION THROUGH MALTOPORIN CHANNELS AT 3.1 ANGSTROMS RESOLUTION

Overview

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.

About this Structure

1MAL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution., Schirmer T, Keller TA, Wang YF, Rosenbusch JP, Science. 1995 Jan 27;267(5197):512-4. PMID:7824948

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