1af6
From Proteopedia
(New page: 200px<br /><applet load="1af6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1af6, resolution 2.4Å" /> '''MALTOPORIN SUCROSE CO...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1af6.gif|left|200px]]<br /><applet load="1af6" size=" | + | [[Image:1af6.gif|left|200px]]<br /><applet load="1af6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1af6, resolution 2.4Å" /> | caption="1af6, resolution 2.4Å" /> | ||
'''MALTOPORIN SUCROSE COMPLEX'''<br /> | '''MALTOPORIN SUCROSE COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Maltoporin (LamB) facilitates the diffusion of maltodextrins across the | + | 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== | ||
| - | 1AF6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1AF6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AF6 OCA]. |
==Reference== | ==Reference== | ||
| Line 22: | Line 22: | ||
[[Category: sugar transport]] | [[Category: sugar transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:43:52 2008'' |
Revision as of 09:43, 21 February 2008
|
MALTOPORIN SUCROSE COMPLEX
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.
About this Structure
1AF6 is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
Channel specificity: structural basis for sugar discrimination and differential flux rates in maltoporin., Wang YF, Dutzler R, Rizkallah PJ, Rosenbusch JP, Schirmer T, J Mol Biol. 1997 Sep 12;272(1):56-63. PMID:9299337
Page seeded by OCA on Thu Feb 21 11:43:52 2008
