What to do while awaiting crystals of a membrane transport protein and thereafter

Accounts of Chemical Research

Volumn 32, Issue 9, 1999, Pages 805-813

  Kaback, H Ronald ^a,b   Wu, Jianhua ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b GENOME THERAPEUTICS CORPORATION   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; BACTERIAL ENZYME; CARRIER PROTEIN; CYSTEINE; GLUTAMINE; LACTOSE PERMEASE; MEMBRANE PROTEIN;

ARTICLE; BACTERIUM MUTANT; ENZYME PURIFICATION; ESCHERICHIA COLI; MEMBRANE TRANSPORT; NONHUMAN; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

EID: 0032819684     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar970256i     Document Type: Article

References (44)

1. Viitanen, P.; Newman, M. J.; Foster, D. L.; Wilson, T. H.; Kaback, H. R. Purification, reconstitution, and characterization of the lac permease of Escherichia coli Methods Enzymol. 1986, 125, 429-452.
2. Sahin-Tóth, M.; Lawrence, M. C.; Kaback, H. R. Properties of permease dimer, a fusion protein containing two lactose permease molecules from Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 5421-5425.
3. Kaback, H. R.; Voss, J.; Wu, J. Helix packing in polytopic membrane proteins: the lactose permease of Escherichia coli. Curr. Opin. Struct. Biol. 1997, 7, 537-542.
4. Kaback, H. R.; Wu, J. From Membrane to Molecule to the Third Amino Acid from the Left with the Lactose Permease of Escherichia coli. Q. Rev. Biophys. 1997, 30, 333-364.
5. Frillingos, S.; Sahin-Tóth, M.; Wu, J.; Kaback, H. R. Cys-scanning mutagenesis: a novel approach to structure-functions relationships in polytopic membrane proteins. FASEB J. 1998, 12, 1281-1299.
6. Pouny, Y.; Weitzman, C.; Kaback, H. R. In vitro biotinylation provides quantitative recovery of highly purified active lactose permease in a single step. Biochemistry 1998, 37, 15713-15719.
7. Privé, G. G.; Kaback, H. R. Engineering the lac permease for purification and crystallization. J. Bioenerg. Biomem. 1996, 28, 29-34.
8. Wu, J.; Kaback, H. R. A general method for determining helix packing in membrane proteins in situ: helices I and II are close to helix VII in the lactose permease of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 14498-14502.
9. Wu, J.; Kaback, H. R. Helix proximity and ligand-induced conformational changes in the lactose permease of Escherichia coli determined by site-directed chemical crosslinking. J. Mol. Biol. 1997, 270, 285-293.
10. Wu, J.; Hardy, D.; Kaback, H. R. Transmembrane helix tilting and ligand-induced conformational changes in the lactose permease determined by site-directed chemical crosslinking in situ. J. Mol. Biol. 1998, 282, 959-967.
11. Wu, J.; Hardy, D.; Kaback, H. R. Tilting of helix I and ligand-induced changes in the lactose permease determined by site-directed chemical cross-linking in situ. Biochemistry 1998, 37, 15785-15790.
12. Wu, J.; Hardy, D.; Kaback, H. R. Site-directed chemical crosslinking demonstrate that helix IV is close to helices VII and XI in the lactose permease. Biochemistry 1998, 30, 1715-1720.
13. Wu, J.; Hardy, D.; Kaback, H. R. Tertiary contacts of helix V in the lactose permease determined by site-directed chemical crosslinking in situ. Biochemistry 1998, 38, 2320-2325.
14. Sahin-Tóth, M.; Dunten, R. L.; Kaback, H. R. Design of a membrane protein for site-specific proteolysis: properties of engineered factor Xa protease sites in the lactose permease of Escherichia coli. Biochemistry 1995, 34, 1107-1112.
15. Zen, K.; Consler, T. G.; Kaback, H. R. Insertion of the polytopic membrane protein lactose permease occurs by multiple mechanisms. Biochemistry 1995, 34, 3430-3437.
16. Wu, J.; Voss, J.; Hubbell, W. L.; Kaback, H. R. Site-directed spin labeling and chemical crosslinking demonstrate that helix V is close to helicies VII and VIII in the lactose permease of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 10123-10127.
17. Sun, J.; Kaback, H. R. Proximity of periplasmic loops in the lactose permease of Escherichia coli determined by site-directed crosslinking. Biochemistry 1997, 36, 11959-11965.
18. Akabas, M. H.; Stauffer, D. A.; Xu, M.; Karlin, A. Acetylcholine receptor channel structure probed in cysteine-substitution mutants. Science 1992, 258, 307-310.
19. Zhuang, J.; Privé, G. G.; Verner, G. E.; Ringler, P.; Kaback, H. R.; Engel, A. Two-dimentional crystallization of the Escherichia coli lactose permease. J. Struct. Biol., in press.
20. Jung, H.; Jung, K.; Kaback, H. R. Cysteine 148 in the lactose permease of Escherichia coli is a component of a substrate binding site. I. Site-directed mutagenesis studies. Biochemistry 1994, 33, 12160-12165.
21. Wu, J.; Kaback, H. R. Cysteine 148 in the lactose permease of Escherichia coli is a component of a substrate binding site. 2. Site-directed fluorescence studies. Biochemistry 1994, 33, 12166-12171.
22. Frillingos, S.; Kaback, H. R. Probing the conformation of the lactose permease of Escherichia coli by in situ site-directed sulfhydryl modification. Biochemistry 1996, 35, 3950-3956.
23. Frillingos, S.; Wu, J.; Venkatesan, P.; Kaback, H. R. Binding of ligand or monoclonal antibody 4B1 induces discrete structural changes in the lactose permease of Escherichia coli. Biochemistry 1997, 36, 6408-6414.
24. Frillingos, S.; Kaback, H. R. The role of helix VIII in the lactose permease of Escherichia coli. II. Site-directed sulfhydryl modification. Protein Sci. 1997, 6, 438-443.
25. Frillingos, S.; Gonzalez, A.; Kaback, H. R. Cysteine-scanning mutagenesis of helix IV and the adjoining loops in the lactose permease of Escheichia coli: Glu126 and Arg144 are essential. Biochemistry 1997, 36, 14284-14290.
26. Sahin-Tóth, M.; le Coutre, J.; Kharabi, D.; le Maire, G.; Lee, J. C.; Kaback, H. R. Characterization of Glu126 and Arg144, two residues that are indispensable for substrate binding in the lactose permease of Escherichia coli. Biochemistry 1998, 38, 813-819.
27. Venkatesan, P.; Kaback, H. R. The substrate binding site in the lactose permease of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 9802-9807.
28. le Coutre, J.; Narasimhan, L. R.; Patel, C. K.; Kaback, H. R. The lipid bilayer determines helical tilt angle and function in lactose permease of Eschrichia coli. Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 10167-10171.
29. + channel. Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 6114-6117.
30. Alvarez, J.; Lee, D. C.; Baldwin, S. A.; Chapman, D. Fourier transform infrared spectroscopic study of the structure and conformational changes of the human erythrocyte glucose transporter. J. Biol. Chem. 1987, 262, 3502-3509.
31. Arkin, I. T.; Russ, W. P.; Lebendiker, M.; Schuldiner, S. Determining the secondary structure and orientation of EmrE, a multi-drug transporter, indicates a transmembrane four-helix bundle. Biochemistry 1996, 35, 7233-7238.
32. Downer, N. W.; Bruchman, T. J.; Hazzard, J. H. Infrared spectroscopic study of photoreceptor membrane and purple membrane. Protein secondary structure and hydrogen deuterium exchange. J. Biol. Chem. 1986, 261, 3640-3647.
33. Ujwal, M. L; Sahin-Tóth, M.; Persson, B.; Kaback, H. R. Role of glutamate-269 in the lactose permease of Escherichia coli. Mol. Membr. Biol. 1994, 1, 9-16.
34. Franco, P. J.; Brooker, R. J. Functional roles of Glu-269 and Glu-325 within the lactose permease of Escherichia coli. J. Biol. Chem. 1994, 269, 7379-7386.
35. Viitanen, P.; Garcia, M. L.; Foster, D. L; Kaczorowski, G. J.; Kaback, H. R. Mechanism of lactose translocation in proteoliposomes reconstituted with lac carrier protein purified from Escherichia coli. 2. Deuterium solvent isotope effects. Biochemistry 1983, 22, 2531-2536.
36. Carrasco, N.; Viitanen, P.; Herzlinger, D.; Kaback, H. R. Monoclonal antibodies against the lac carrier protein from Escherichia coli. 1. Functional studies. Biochemistry 1984, 23, 3681-3687.
37. a of a carboxylic acid at position 325 (helix X) of the lactose permease of Escherichia coli. Biochemistry 1996, 35, 10166-10171.
38. 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 of Escherichia coli. Biochemistry 1996, 35, 990-998.
39. Voss, J.; Sun, J.; Kaback, H. R. Sulfhydryl oxidation of mutants with cysteine in place of acidic residues in the lactose permease. Biochemistry 1998, 37, 8191-8196.
40. Sahin-Tóth, M.; Kaback, H. R. Properties of interacting aspartic acid and lysine residues in the lactose permease of Escherichia coli. Biochemistry 1993,32, 10027-10035.
41. Dunten, R. L.; Sahin-Tóth, M.; Kaback, H. R. Role of the charge pair formed by aspartic acid 237 and lysine 358 in the lactose permease of Escherichia coli. Biochemistry 1993, 32, 3139-3145.
42. He, M.; Kaback, H. R. Interaction between residues Glu269 (Helix VIII) and His322 (Helix X) of the lactose permease of Escherichia coli is essential for substrate binding. Biochemistry 1997, 36, 13688-13692.
43. Wolin, C. D. Kaback, H. R. Estimating loop-helix interfaces in a polytopic membrane protein by deletion analysis. Biochemistry, in press.
44. Zhao, M.; Zeu, K.-e.; Hubbell, W. L.; Kaback, H. R. Proximity between Glu126 and Arg144 in the lactose permease of Escherichia coli. Biochemistry, in press.