Two-dimensional crystallization of Escherichia coli lactose permease

Journal of Structural Biology

Volumn 125, Issue 1, 1999, Pages 63-75

  Zhuang, Jianping ^a   Privé, Gilbert G ^b   Werner, Gillian E ^b   Ringler, Philippe ^a   Kaback, H Ronald ^b   Engel, Andreas ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Electron crystallography; Lactose permease fusion protein

Indexed keywords

BACTERIAL ENZYME; CYTOCHROME B; HYBRID PROTEIN; LACTOSE PERMEASE; PHOSPHOLIPID;

ARTICLE; CALCULATION; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; ELECTRON MICROSCOPY; ENZYME ISOLATION; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; STRUCTURE ANALYSIS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0032798465     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1998.4059     Document Type: Article

References (39)

1. Aebi U., Smith P. R., Dubochet J., Henry C., Kellenberger E. A study of the structure of the T-layer ofBacillus brevis. J. Supramol. Struct. 1:1973;498-522.
2. Baschong W., Wrigley N. G. Small colloidal gold conjugated to Fab fragments or to immunoglobulin G as high-resolution labels for electron microscopy: A technical overview. J. Electron. Microsc. Tech. 14:1990;313-323.
3. Bretaudiere J. P., Frank J. Reconstitution of molecule images analysed by correspondence analysis: A tool for structural interpretation. J. Microsc. 144:1986;1-14.
4. Cabiaux V., Oberg K. A., Pancoska P., Walz T., Agre P., Engel A. Secondary structures comparison of Aquaporin-1 and bacteriorhodopsin: A Fourier transform infrared spectroscopy study of two-dimensional membrane crystals. Biophys. J. 73:1997;406-417.
5. Carrasco N., Viitanen P., Herzlinger D., Kaback H. R. Monoclonal antibodies against the lac carrier protein fromEscherichia coli. Biochemistry. 23:1984;3681-3687.
6. Costello M. J., Escaig J., Matsushita K., Viitanen P. V., Menick D. R., Kaback H. R. Purified lac permease and cytochrome o oxidase are functional as monomers. J. Biol. Chem. 262:1987;17072-17082.
7. Dolder M., Engel A., Zulauf M. The micelle to vesicle transition of lipids and detergents in the presence of a membrane protein: Towards a rationale for 2D crystallization. FEBS Lett. 382:1996;203-208.
8. Frank J., Verschoor A., Boublik M. Computer averaging of electron micrographs of 40S ribosomal subunits. Science. 214:1981;1353-1355.
9. Frillingos S., Gonzalez A., Kaback H. Cysteine-scanning mutagenesis of helix IV and the adjoining loops in the lactose permease ofEscherichia coli: Biochemistry. 47:1998a;14284-14290.
10. aEscherichia coli. Biochemistry. 35:1996;10166-10171.
11. Frillingos S., Sahin-Toth M., Wu J., Kaback H. R. Cys-scanning mutagenesis: A novel approach to structure-functions relationships in polytopic membrane proteins. FASEB J. 12:1998b;1281-1299.
12. Jap B. K., Zulauf M., Scheybani T., Hefti A., Baumeister W., Aebi U., Engel A. 2D crystallization: From art to science. Ultramicroscopy. 46:1992;45-84.
13. Kaback H. R. Molecular biology and energetics of membrane transport. J. Cell Physiol. 89:1976;575-593.
14. Kaback H. R. The lac carrier protein inEscherichia coli. J. Membr. Biol. 76:1983;95-112.
15. Kaback H. R. The lactose permease ofEscherichia coli: Handbook of Biological Physics: Transport Processes in Eukaryotic and Prokaryotic Organisms. 1996;Elsevier, Amsterdam. p. 203-227.
16. Kaback H. R. A molecular mechanism for energy coupling in a membrane transport protein, the lactose permease ofEscherichia coli. Proc. Natl. Acad. Sci. USA. 94:1997;5539-5543.
17. Kaback H. R., Voss J., Wu J. Helix packing in polytopic membrane proteins: The lactose permease ofEscherichia coli. Curr. Opin. Struct. Biol. 7:1997;537-542.
18. Kaback H. R., Wu J. From membrane to molecule to the third amino acid from the left with a membrane transport protein. Q. Rev. Biophys. 30:1997;333-364.
19. Le Coutre J., Narasimhan L. R., Kumar C., Patel N., Kaback H. R. The lipid bilayer determines helical tilt angle and function in lactose permease ofEscherichia coli. Proc. Natl. Acad. Sci. USA. 94:1997;10167-10171.
20. Li J., Tooth P. Size and shape of theEscherichia coli. Biochemistry. 26:1987;4816-4823.
21. Loddenkotter B., Kammerer B., Fischer K., Flügge U.-I. Expression of the functional mature chloroplast triose phosphate translocator in yeast internal membrane and purification of the histidine-tagged protein by a single metal-affinity chromatography step. Proc. Natl. Acad. Sci. USA. 90:1993;2155-2159.
22. Mathews F. S., Bethge P. H., Czerwinski E. W. The structure of cytochrome b562 fromEscherichia coli. J. Biol. Chem. 254:1979;1699-1706.
23. Page M. G., Rosenbusch J. P., Yamato I. The effects of pH on proton sugar symport activity of the lactose permease purified fromEscherichia coli. J. Biol. Chem. 263:1988;15897-15905.
24. Poolman B., Konings W. N. Secondary solute transport in bacteria. Biochim. Biophy. Acta. 1183:1993;5-39.
25. Privé G. G., Verner G. E., Weitzman C., Zen K. H., Eisenberg D., Kaback H. R. Fusion proteins as tools for crystallization: The lactose permease fromEscherichia coli. Acta Crystallogr. 50:1994;375-379.
26. Rigaud J. L., Mosser G., Lacapere J. J., Olofsson A., Levy D., Ranck J. L. Bio-Beads: An efficient strategy for two-dimensional crystallization of membrane proteins. J. Struct. Biol. 118:1997;226-235.
27. Rigaud J. L., Pitard B., Levy D. Reconstitution of membrane proteins into liposomes: Application to energy-transducing membrane proteins. Biochim. Biophys. Acta. 1231:1995;223-246.
28. Sahin-Tóth M., Lawrence M. C., Kaback H. R. Properties of permease dimer, a fusion protein containing two lactose permease molecules fromEscherichia coli. Proc. Natl. Acad. Sci. USA. 91:1994;5421-5425.
29. Saxton W. O., Baumeister W. The correlation averaging of a regularly arranged bacterial cell envelope protein. J. Microsc. 127:1982;127-138.
30. Saxton W. O., Pitt J. T., Horner M. Digital image processing: The Semper system. Ultramicroscopy. 4:1979;343-354.
31. Sun J., Wu J., Carrasco N., Kaback H. R. Identification of the epitope for monoclonal antibody 4B1 which uncouples lactose and proton translocation in the lactose permease ofEscherichia coli. Biochemistry. 35:1996;990-998.
32. Takayama M., Itoh S., Nagasaki T., Tanimizu I. A new enzymatic method for determination of serum choline-containing phospholipids. Clin. Chim. Acta. 79:1977;93-98.
33. Thuman-Commike P. A., Chiu W. PTOOL: A software package for the selection of particles from electron cryomicroscopy spot-scan images. J. Struct. Biol. 116:1996;41-47.
34. Unser M., Trus B. L., Steven A. C. A new resolution criterion based on spectral signal-to-noise ratios. Ultramicroscopy. 23:1987;39-52.
35. van Heel M. Multivariate statistical classification of noise images (randomly oriented biological macromolecules). Ultramicroscopy. 13:1984;165-184.
36. Venkatesan P., Kaback H. R. The substrate-binding site in the lactose permease ofEscherichia coli. Proc. Natl. Acad. Sci. USA. 95:1998;9802-9807.
37. Viitanen P., Newman M. J., Foster D. L., Wilson T. H., Kaback H. R. Purification, reconstitution, and characterization of the lac permease ofEscherichia coli. Methods Enzymol. 125:1986;429-452.
38. Voss J., Hubbell W. L., Kaback H. R. Helix packing in the lactose permease determined by metal-nitroxide interaction. Biochemistry. 37:1998;211-216.
39. Walz T., Hirai T., Murata K., Heymann J. B., Mitsuoka K., Fujiyoshi Y., Smith B. L., Agre P., Engel A. The three-dimensional structure of aquaporin-1. Nature. 387:1997;624-627.