• References
• Sucrose Specific Porin
• Slides

References

1. Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose. Forst, Doris, Welte, Wolfram, Wacker, Thomas, Diedrichs, Kay. Nature Structural Biology. 5(1): 37-45. 1998.

2. Permeation of hydrophilic molecules through the outer membrane of gram-negative bacteria. Benz, R., Bauer, K. Eur.J.Biochem. 176: 1-19. 1988.

3. Characterization of the major envelope protein from Escherichia coli. Rosenbusch, J.P. J. Biol. Chem. 249: 8019-8029. 1974.

4. Derepression of LamB protein facilitates outer membrane permeation of carbohydrates into Escherichia coli under conditions of nutrient stress. Death, A., Notley, L., Ferenci, T. J. Bacteriol. 175: 1475-1483. 1993.

5. Plasmid-mediated uptake and metabolism of sucrose by Escherichia coli K-12. Schmid, K., Schupfner, M., Schmitt, R. J. Bacteriol. 151: 68-76. 1982.

6. Constants of Sugar Transport Through Two LamB Mutants of Escherichia coli: Comparison with Wild-type Maltoporin and LamB of Salmonella typhimurium. Jordy, M., Andersen, C., Schülein, K., Ferenci, T., Benz, R. J. Mol. Biol. 259: 666-678. 1996.

7. Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution. Schirmer, T., Keller, T.A., Wang, Y., Rosenbusch, J.P. Science. 267: 512-514. 1995.

8. Channel specificity: Structural basis for sugar discrimination and differential flux rates in maltoporin. Wang, Y.-F., Dutzler, R., Rizkallah, P.J., Rosenbusch, J.P., Schirmer, T. J. Mol. Biol. 272: 56-63. 1997.

9. Crystal structures of the various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway. Dutzler, R., Wang, Y.-F., Rizkallah, P.J., Rosenbusch, J.P., Schirmer, T. Structure. 4: 127-134. 1996.

10. Study of sugar binding to the sucrose-specific ScrY Channel of enteric bacteria using current noise analysis. Anderson, C., R. Csech, K Schulein, R. Benz. Membrane Biology. 164: 263-274. 1997.

11. Holm L, Rosenström P (2010) Dali server: conservation mapping in 3D. Nucl. Acids Res. 38: 545-549.

12. A sugar-specific porin, ScrY, is involved in sucrose uptake in enteric bacteria. Schmid, K., Ebner, R., Jahreis, K., Lengeler, J.W., Titgemeyer, F. Mol. Microbiol. 5: 941-950. 1991.

13. The deletion of 70 amino acids near the N-terminal end of the sucrose-specific porin ScrY causes its functional similarity to LamB in vivo and in vitro. Schülein, K., Andersen, C., Benz, R. Mol. Microbiol. 17: 757-767. 1995.

14. Structure of a Legume Lectin with an Ordered N-linked Carbohydrate in Complex with Lactose. Shaanan, B., Lis, H., Sharon, N. Science. 254: 862-866. 1991.

15. Electrostatic interactions in aromatic oligopeptides contribute to protein stability. Burley, S.K., Petsko, G.A. TIBTECH. 7: 354-359. 1989.