1mal: Difference between revisions

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[[Image:1mal.~~jpg~~|left|200px]]

[[Image:1mal.png|left|200px]]

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

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

~~==Overview==~~

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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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_7824948}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 7824948 is the PubMed ID number.

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==About this Structure==

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[[Category: Schirmer, T.]]

[[Category: Outer membrane protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May~~ ~~3 00~~:49:54 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:34:12 2008''

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-[[Image:1mal.jpg|left|200px]]
+{{Seed}}
+[[Image:1mal.png|left|200px]]
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 {{STRUCTURE_1mal|  PDB=1mal  |  SCENE=  }}
-'''STRUCTURAL BASIS FOR SUGAR TRANSLOCATION THROUGH MALTOPORIN CHANNELS AT 3.1 ANGSTROMS RESOLUTION'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_7824948}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7824948 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7824948}}
 ==About this Structure==
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 [[Category: Schirmer, T.]]
 [[Category: Outer membrane protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:49:54 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 23:34:12 2008''