Channel specificity: Structural basis for sugar discrimination and differential flux rates in maltoporin

Journal of Molecular Biology

Volumn 272, Issue 1, 1997, Pages 56-63

  Wang, Yan Fei ^a,c   Dutzler, Raimund ^a   Rizkallah, Pierre J ^b   Rosenbusch, Jurg P ^a   Schirmer, Tilman ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

^b DARESBURY LABORATORY   (United Kingdom)

^c MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

Author keywords

Facilitated diffusion; Outer membrane protein; Sugar transport; X ray structure

Indexed keywords

DISACCHARIDE; MALTODEXTRIN; MELIBIOSE; OUTER MEMBRANE PROTEIN; PORIN; SUCROSE; TREHALOSE;

ARTICLE; DIFFUSION; ESCHERICHIA COLI; MEMBRANE CHANNEL; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ANALYSIS; SUGAR TRANSPORT;

ESCHERICHIA COLI;

EID: 0031565721     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1224     Document Type: Article

References (31)

1. Andersen C., Jordy M., Benz R. Evaluation of the rate constants of sugar transport through maltoporin (LamB) ofE. coli. J. Gen. Physiol. 105:1995;385-401.
2. Benson S. A., Occi J. L. L., Sampson B. A. Mutations that alter the pore function of the OmpF porin ofEscherichia coli. J. Mol. Biol. 203:1988;961-970.
3. Benz R., Schmid A., Greetje H., Vos-Scheperkeuter H. Mechanism of sugar transport through the sugar-specific LamB channel ofEscherichia coli. J. Membr. Biol. 100:1987;21-29.
4. Boos W., Ehmann U., Forkl H., Klein W., Rimmele M., Postma P. Trehalose transport and metabolism inEscherichia coli. J. Bacteriol. 172:1990;3450-3461.
5. Brünger A. T. FreeR. Nature. 355:1992a;472-475.
6. Brünger A. T. X-PLOR Manual. version 3.1. 1992b;Yale University, New Haven.
7. Burling F. T., Weis W. I., Flaherty K. M., Brünger A. T. Direct observation of protein solvation and discrete disorder with experimental crystallographic phases. Science. 271:1996;72-77.
8. Collaborative computational project number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
9. Death A., Notley L., Ferenci T. De-repression of LamB protein facilitates outer membrane permeation of carbohydrates intoEscherichia coli. J. Bacteriol. 175:1993;1475-1483.
10. Dominguez R., Souchon H., Lascombe M.-B., Alzari P. M. The crystal structure of a family five endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism. J. Mol. Biol. 257:1996;1042-1051.
11. Dutzler R., Wang Y.-F., Rizkallah P. J., Rosenbusch J. P., Schirmer T. Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway. Structure. 4:1996;127-134.
12. Forst D., Schülein K., Wacker T., Diederichs K., Kreutz W., Benz R., Welte W. Crystallization and preliminary X-ray diffraction analysis of ScrY, a specific bacterial outer membrane porin. J. Mol. Biol. 229:1993;258-262.
13. Hardesty C., Ferran C., Dirienzo J. M. Plasmid-mediated sucrose metabolism inEscherichia coliscrY. J. Bacteriol. 173:1991;449-456.
14. Jones T. A., Kjeldgaard M. Manual for O. 1991;Uppsala University, Uppsala.
15. Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallog. 26:1993;795-800.
16. Keller T. A., Ferenci T., Prilipov A., Rosenbusch J. P. Crystallization of monodisperse maltoporin from wild-type and mutant strains of variousEnterobacteriaceae. Biochem. Biophys. Res. Commun. 199:1994;767-771.
17. Klein W., Boos W. Induction of the λ-receptor is essential for effective uptake of trehalose inEscherichia coli. J. Bacteriol. 175:1993;1682-1686.
18. Kleywegt G. J., Jones T. A. From First Map to Final Map. 1994;SERC Daresbury Laboratory, Daresbury.
19. Leslie A. G. W. Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography. 1992;Daresbury Laboratory, Warrington.
20. Luckey M., Nikaido H. Specificity of diffusion channels produced by lambda phage receptor protein ofEscherichia coli. Proc. Natl Acad. Sci. USA. 77:1980;167-171.
21. Meyer J. E. W., Hofnung M., Schulz G. E. Structure of maltoporin fromSalmonella typhimurium. J. Mol. Biol. 266:1997;761-775.
22. Nikaido H. Porins and specific diffusion channels in bacterial outer membranes. J. Biol. Chem. 269:1994;3905-3908.
23. Nikaido H., Saier M. H. J. Transport proteins in bacteria: common themes in their design. Science. 258:1992;936-942.
24. Rosenbusch J. P. Konings W. N., Kaback H. R., Lolkema J. S. Handbook of Biological Physics. 1996;Elsevier Science B.V. Amsterdam.
25. Schirmer T., Keller T. A., Wang Y.-F., Rosenbusch J. P. Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution. Science. 267:1995;512-514.
26. Schmid K., Ebner R., Altenbucher J., Schmitt R., Lengeler J. W. Plasmid-mediated sucrose metabolism inEscherichia coli. Mol. Microbiol. 2:1988;1-8.
27. Schmid K., Ebner R., Jahreis K., Lengeler J. W., Titgemeyer F. A sugar-specific porin, ScrY, is involved in sucrose uptake in enteric bacteria. Mol. Microbiol. 5:1991;941-950.
28. Schülein K., Schmid K., Benz R. The sugar-specific outer membrane channel ScrY contains functional characteristics of general diffusion pores and substrate specific porins. Mol. Microbiol. 5:1991;2233-2241.
29. Schulz G. E. Porins: general to specific, native to engineered passive pores. Curr. Opin. Struct. Biol. 6:1996;485-490.
30. Schwartz M. Neidhardt F. C. In Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology. 1987;American Society of Microbiology, Washington.
31. Spurlino J. C., Lu G.-Y., Quiocho F. A. The 2.3 Å resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J. Biol. Chem. 266:1991;5202-5219.