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1AF6

MALTOPORIN SUCROSE COMPLEX

Summary for 1AF6
Entry DOI10.2210/pdb1af6/pdb
Related PRD IDPRD_900003
DescriptorMALTOPORIN, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordsmembrane protein, specific porin, beta barrel, sugar transport, sucrose
Biological sourceEscherichia coli
Cellular locationCell outer membrane; Multi-pass membrane protein: P02943
Total number of polymer chains3
Total formula weight143401.47
Authors
Dutzler, R.,Schirmer, T. (deposition date: 1997-03-21, release date: 1998-03-25, Last modification date: 2024-10-30)
Primary citationWang, 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: 9299337
DOI: 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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