1mal
From Proteopedia
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|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mal OCA], [http://www.ebi.ac.uk/pdbsum/1mal PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mal RCSB]</span> | ||
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[[Category: outer membrane protein]] | [[Category: outer membrane protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:13:40 2008'' |
Revision as of 19:13, 30 March 2008
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| , resolution 3.10Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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