Crystal structures and solution conformations of a dominant-negative mutant of Escherichia coli maltose-binding protein

Journal of Molecular Biology

Volumn 264, Issue 2, 1996, Pages 364-376

  Shilton, Brian H ^a,c   Shuman, Howard A ^b   Mowbray, Sherry L ^a  

^a SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

^b New York Presbyterian Columbia University Medical Center   (United States)

^c NATIONAL RESEARCH COUNCIL CANADA   (Canada)

Author keywords

Conformational change; Kinetic modelling; Ligand transport; Periplasmic binding proteins

Indexed keywords

ARGININE; MALTOSE; MALTOSE BINDING PROTEIN; MUTANT PROTEIN; TRYPTOPHAN;

ARTICLE; CARBOHYDRATE TRANSPORT; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN PURIFICATION; STEREOCHEMISTRY; SUGAR TRANSPORT; X RAY CRYSTALLOGRAPHY;

ESCHERICHIA COLI;

EID: 0030606256     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0646     Document Type: Article

References (38)

1. Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer, E. T. J., Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T. & Tasumi, M. (1977). The Protein Data Bank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 112, 535-542.
2. Bohl, E., Shuman, H. A. & Boos, W. (1995). Mathematical treatment of the kinetics of binding protein dependent transport systems reveals that both the substrate loaded and unloaded binding proteins interact with the membrane components. J. Theor. Biol. 172, 83-94.
3. Brünger, A. T. (1992). X-PLOR: A System for X-ray Crystallography and NMR, Yale University Press, New Haven.
4. Brünger, A. T., Kuriyan, J. & Karplus, M. (1987). Crystallographic R-factor refinement by molecular dynamics. Science, 235, 458-460.
5. CCP4 (1979). The SERC (UK) Collaborative Computing Project no. 4: a Suite of Programs for Protein Crystallography, Daresbury Laboratory, Warrington WA4 4AD, UK.
6. Davidson, A. L. & Nikaido, H. (1990). Overproduction, solubilization, and reconstitution of the maltose transport system from Escherichia coli. J. Biol. Chem. 265, 4254-4260.
7. Davidson, A. L., Shuman, H. A. & Nikaido, H. (1992). Mechanism of maltose transport in Escherichia coli: transmembrane signaling by periplasmic binding proteins. Proc. Natl Acad. Sci. USA, 89, 2360-2364.
8. Dean, D. A., Fikes, F. D., Gehring, K., Bassford, P. J. J. & Nikaido, H. (1989). Active transport of maltose in membrane vesicles obtained from Escherichia coli cells producing tethered maltose-binding protein. J. Bacteriol. 171, 503-510.
9. Dean, D. A., Hor, L. I., Shuman, H. A. & Nikaido, H. (1992). Interaction between maltose-binding protein and the membrane-associated maltose transporter complex in Escherichia coli. Mol. Microbiol. 6, 2033-2040.
10. Duplay, P., Bedouelle, H., Fowler, A., Zabin, I., William, S. & Hofnung, M. (1984). Sequences of the malE gene and of its product, the maltose-binding protein of Escherichia coli K12. J. Biol. Chem. 259, 10606-10613.
11. Ferenci, T. & Klotz, U. (1978). Affinity Chromatographic isolation of the periplasmic maltose binding protein of Escherichia coli. FEBS Letters, 94, 213-217.
12. Flocco, M. M. & Mowbray, S. L. (1994). The 1.9 Å X-ray structure of a closed unliganded form of the periplasmic glucose/galactose receptor from Salmonella typhimurium. J. Biol. Chem. 269, 8931-8936.
13. 2 membrane transport complex. J. Mol. Biol. 233, 659-670.
14. Jones, T. A. & Kjeldgaard, M. O. (1995). O: The Manual. Version 9, Uppsala, Sweden.
15. Keidel, S., Rupp, E. & Szardenings, M. (1992). Recombinant human retinoic acid receptor α. Binding of DNA and synthetic retinoids to the protein expressed in Escherichia coli. Eur. J. Biochem. 204, 1141-1148.
16. Kraulis, P. (1991). Molscript: a program to produce both detailed and schematic plots of, protein structures. J. Appl. Crystallog. 24, 946-950.
17. Koiwai, O. & Hayashi, H. (1979). Studies on bacterial chemotaxis: IV. Interaction of maltose receptor with a membrane-bound chemosensing component. J. Biochem. 86, 27-34.
18. Lakiwicz, J. R. (1983). Principles of Fluorescence Spectroscopy, pp. 260-290, Plenum Press, New York.
19. Martineau, P., Szmelcman, S., Spurlino, J. C., Quiocho, F. A. & Hofnung, M. (1990). Genetic approach to the role of tryptophan residues in the activities and fluorescence of a bacterial periplasmic maltose-binding protein. J. Mol. Biol. 214, 337-352.
20. Merino, G., Boos, W., Shuman, H. & Bohl, E. (1995). The inhibition of maltose transport by the unliganded form of the maltose-binding protein of Escherichia coli: experimental findings and mathematical treatment. J. Theor. Biol. 177, 171-179.
21. Miller, D. M., Olson, J. S., Pflugrath, J. W. & Quiocho, F. A. (1983). Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis. J. Biol. Chem. 258, 13665-13672.
22. Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A, 50, 157-163.
23. Neu, H. C. & Heppel, L. A. (1965). The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts. J. Biol. Chem. 240, 3685-3692.
24. Otwinowski, Z. (1991). Data Collection and Processing (Sawyer, L., Isaacs, N. & Burley, S., eds), pp. 56-62, Proc. CCP4 Study Weekend, 29-30 Jan 1991, SERC Daresbury Laboratory, UK.
25. Sharff, A. J., Rodseth, L. E., Spurlino, J. C. & Quiocho, F. A. (1992). Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis. Biochemistry, 31, 10657-10663.
26. Sharff, A. J., Rodseth, L. E. & Quiocho, F. A. (1993). Refined 1.8-Å structure reveals the mode of binding of β-cyclodextrin to the maltodextrin binding protein. Biochemistry, 32, 10553-10559.
27. Sharff, A. J., Rodseth, L. E., Hofnung, M., Szmelcman, S. & Quiocho, F. A. (1994). Refined structures of two insertion/deletion mutants probe function of maltose binding protein. J. Mol. Biol. 246, 8-13.
28. Shilton, B. H. & Mowbray, S. L. (1995). Simple models for the analysis of binding protein-dependent transport systems. Protein Sci. 4, 1346-1355.
29. Shilton, B. H., Flocco, M. M., Nilsson, M. & Mowbray, S. L. (1996). Conformational changes of three periplasmic receptors for bacterial chemotaxis and transport: The maltose-, glucose/galactose-and ribose-binding proteins. J. Mol. Biol. 264, 350-363.
30. Shuman, H. A. (1982). Active transport of maltose in Escherichia coli K12. J. Biol. Chem. 257, 5455-5461.
31. Spurlino, J. C., Lu, G.-Y. & Quiocho, F. A. (1991). 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, 5202-5219.
32. Spurlino, J. C., Rodseth, L. E. & Quiocho, F. A. (1992). Atomic interactions in protein-carbohydrate complexes. Tryptophan residues in the periplasmic maltodextrin receptor for active transport and chemotaxis. J. Mol. Biol. 226, 15-22.
33. Szmelcman, S., Schwartz, M., Silhavy, T. J. & Boos, W. (1976). Maltose transport in Escherichia coli K12. A comparison of transport kinetics in wild-type and lambda-resistant mutants as measured by fluorescence quenching. Eur. J. Biochem. 65, 13-19.
34. Treptow, N. A. & Shuman, H. A. (1985). Genetic evidence for substrate and periplasmic-binding-protein recognition by the MalF and MalG proteins, cytoplasmic membrane components of the Escherichia coli maltose transport system. J. Bacteriol. 163, 654-660.
35. Treptow, N. A. & Shuman, H. A. (1988). Allele-specific malE mutations that restore interactions between maltose-binding protein and the inner-membrane components of the maltose transport system. J. Mol. Biol. 202, 809-822.
36. Vonrhein, C., Schlauderer, G. J. & Schulz, G. E. (1995). Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases. Structure, 3, 483-490.
37. Zhang, X., Wozniak, J. A. & Matthews, B. W. (1995). Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme. J. Mol. Biol. 250, 527-552.
38. Zhang, Y., Mannering D. E., Davidson, A. L. & Manson, M. D. (1996). Maltose-binding protein containing an interdomain disulfide bridge confers a dominant-negative phenotype for transport and chemotaxis. J. Biol. Chem. 271, 17881-17889.