1mpq: Difference between revisions

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New page: left|200px<br /><applet load="1mpq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mpq, resolution 3.0Å" /> '''MALTOPORIN TREHALOSE ...
 
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[[Image:1mpq.jpg|left|200px]]<br /><applet load="1mpq" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1mpq.jpg|left|200px]]<br /><applet load="1mpq" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1mpq, resolution 3.0&Aring;" />
caption="1mpq, resolution 3.0&Aring;" />
'''MALTOPORIN TREHALOSE COMPLEX'''<br />
'''MALTOPORIN TREHALOSE COMPLEX'''<br />


==Overview==
==Overview==
Maltoporin (LamB) facilitates the diffusion of maltodextrins across the, outer membrane of E. coli. The structural basis for the specificity of the, channel is investigated by X-ray structure analysis of maltoporin in, complex with the disaccharides sucrose, trehalose, and melibiose. The, sucrose complex, determined to 2.4 A resolution, shows that the glucosyl, moiety is partly inserted into the channel constriction, while the bulky, fructosyl residue appears to be hindered to enter the constriction, thus, interfering with its further translocation. One of the glucosyl moieties, of trehalose is found in a similar position as the glucosyl moiety of, sucrose, whereas melibiose appears disordered when bound to maltoporin. A, comparison with the previously reported maltoporin-maltose complex sheds, light on the basis for sugar discrimination, and explains the different, permeation rates observed for the saccharides.
Maltoporin (LamB) facilitates the diffusion of maltodextrins across the outer membrane of E. coli. The structural basis for the specificity of the channel is investigated by X-ray structure analysis of maltoporin in complex with the disaccharides sucrose, trehalose, and melibiose. The sucrose complex, determined to 2.4 A resolution, shows that the glucosyl moiety is partly inserted into the channel constriction, while the bulky fructosyl residue appears to be hindered to enter the constriction, thus interfering with its further translocation. One of the glucosyl moieties of trehalose is found in a similar position as the glucosyl moiety of sucrose, whereas melibiose appears disordered when bound to maltoporin. A comparison with the previously reported maltoporin-maltose complex sheds light on the basis for sugar discrimination, and explains the different permeation rates observed for the saccharides.


==About this Structure==
==About this Structure==
1MPQ 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MPQ OCA].  
1MPQ 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=1MPQ OCA].  


==Reference==
==Reference==
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[[Category: sugar transport]]
[[Category: sugar transport]]


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