1AF6
MALTOPORIN SUCROSE COMPLEX
Summary for 1AF6
Entry DOI | 10.2210/pdb1af6/pdb |
Related PRD ID | PRD_900003 |
Descriptor | MALTOPORIN, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, MAGNESIUM ION, ... (4 entities in total) |
Functional Keywords | membrane protein, specific porin, beta barrel, sugar transport, sucrose |
Biological source | Escherichia coli |
Cellular location | Cell outer membrane; Multi-pass membrane protein: P02943 |
Total number of polymer chains | 3 |
Total formula weight | 143401.47 |
Authors | Dutzler, R.,Schirmer, T. (deposition date: 1997-03-21, release date: 1998-03-25, Last modification date: 2024-10-30) |
Primary citation | Wang, Y.F.,Dutzler, R.,Rizkallah, P.J.,Rosenbusch, J.P.,Schirmer, T. Channel specificity: structural basis for sugar discrimination and differential flux rates in maltoporin. J.Mol.Biol., 272:56-63, 1997 Cited by PubMed Abstract: 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. PubMed: 9299337DOI: 10.1006/jmbi.1997.1224 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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