1mal
From Proteopedia
(New page: 200px<br /><applet load="1mal" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mal, resolution 3.10Å" /> '''STRUCTURAL BASIS FOR...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1mal.jpg|left|200px]]<br /><applet load="1mal" size=" | + | [[Image:1mal.jpg|left|200px]]<br /><applet load="1mal" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mal, resolution 3.10Å" /> | caption="1mal, resolution 3.10Å" /> | ||
'''STRUCTURAL BASIS FOR SUGAR TRANSLOCATION THROUGH MALTOPORIN CHANNELS AT 3.1 ANGSTROMS RESOLUTION'''<br /> | '''STRUCTURAL BASIS FOR SUGAR TRANSLOCATION THROUGH MALTOPORIN CHANNELS AT 3.1 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Trimeric maltoporin (LamB protein) facilitates the diffusion of | + | 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== | ==About this Structure== | ||
| - | 1MAL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1MAL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAL OCA]. |
==Reference== | ==Reference== | ||
| Line 16: | Line 16: | ||
[[Category: outer membrane protein]] | [[Category: outer membrane protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:53:20 2008'' |
Revision as of 11:53, 21 February 2008
|
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
Page seeded by OCA on Thu Feb 21 13:53:20 2008
