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PDBsum entry 1mal
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Outer membrane protein
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PDB id
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1mal
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References listed in PDB file
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Key reference
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Title
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Structural basis for sugar translocation through maltoporin channels at 3.1 a resolution.
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Authors
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T.Schirmer,
T.A.Keller,
Y.F.Wang,
J.P.Rosenbusch.
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Ref.
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Science, 1995,
267,
512-514.
[DOI no: ]
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PubMed id
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Abstract
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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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Secondary reference #1
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Title
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Crystallization and preliminary X-Ray characterization of maltoporin from escherichia coli.
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Authors
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K.A.Stauffer,
M.G.Page,
A.Hardmeyer,
T.A.Keller,
R.A.Pauptit.
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Ref.
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J Mol Biol, 1990,
211,
297-299.
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PubMed id
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