Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution

Science

Volumn 286, Issue 5438, 1999, Pages 255-260

  Luecke, Hartmut ^a,b   Schobert, Brigitte ^a,b   Richter, Hans Thomas ^a,b   Cartailler, Jean Philippe ^a   Lanyi, Janos K ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; SCHIFF BASE;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ILLUMINATION; ION TRANSPORT; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTON TRANSPORT; STRUCTURE ANALYSIS; X RAY ANALYSIS;

NON-PROGRAMMATIC;

BACTERIORHODOPSINS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; CYTOPLASM; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; ION TRANSPORT; ISOMERISM; LIGHT; MODELS, MOLECULAR; PHOTOLYSIS; PHOTONS; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTON PUMPS; PROTONS; RETINALDEHYDE; SCHIFF BASES; THERMODYNAMICS; WATER;

BACTERIA (MICROORGANISMS);

EID: 0033536594     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.286.5438.255     Document Type: Article

References (54)

1. J. K. Lanyi, J. Struct. Biol. 124, 164 (1998); U. Haupts, J. Tittor, D. Oesterhelt, Annu. Rev. Biophys. Biomol. Struct. 28, 367 (1999).
2. J. K. Lanyi, J. Struct. Biol. 124, 164 (1998); U. Haupts, J. Tittor, D. Oesterhelt, Annu. Rev. Biophys. Biomol. Struct. 28, 367 (1999).
3. E. Pebay-Peyroula, G. Rummel, J. P. Rosenbusch, E. M. Landau, Science 277, 1676 (1997); H. Belrhani et al., Structure 7, 909 (1999).
4. E. Pebay-Peyroula, G. Rummel, J. P. Rosenbusch, E. M. Landau, Science 277, 1676 (1997); H. Belrhani et al., Structure 7, 909 (1999).
5. L. O. Essen, R. Siegert, W. D. Lehmann, D. Oesterhelt, Proc. Natl. Acad. Sci. U.S.A. 95, 11673 (1998).
6. H. Luecke, H. T. Richter, J. K. Lanyi, Science 280, 1934 (1998).
7. Y. Kimura et al., Nature 389, 206 (1997); N. Grigorieff, T. A. Ceska, K. H. Downing, J. M. Baldwin, R. Henderson, J. Mol. Biol. 259, 393 (1996).
8. Y. Kimura et al., Nature 389, 206 (1997); N. Grigorieff, T. A. Ceska, K. H. Downing, J. M. Baldwin, R. Henderson, J. Mol. Biol. 259, 393 (1996).
9. H. Luecke, B. Schobert, H. T. Richter, J.-P. Cartailler, J. K. Lanyi, J. Mol. Biol. 291, 899 (1999).
10. S. Subramaniam, M. Gerstein, D. Oesterhelt, R. Henderson, EMBO J. 12, 1 (1993); J. Vonck, Biochemistry 35, 5870 (1996).
11. S. Subramaniam, M. Gerstein, D. Oesterhelt, R. Henderson, EMBO J. 12, 1 (1993); J. Vonck, Biochemistry 35, 5870 (1996).
12. H. Kamikubo et al., Proc. Natl. Acad. Sci. U.S.A. 93, 1386 (1996).
13. J. K. Lanyi and G. Váró, Israel J. Chem. 35, 365 (1995).
14. S. Dickopf and M. P. Heyn, Biophys. J. 73, 3171 (1997); G. Nagel, B. Kelety, B. Möckel, G. Büldt, E. Bamberg, ibid. 74, 403 (1998).
15. S. Dickopf and M. P. Heyn, Biophys. J. 73, 3171 (1997); G. Nagel, B. Kelety, B. Möckel, G. Büldt, E. Bamberg, ibid. 74, 403 (1998).
16. L. S. Brown, A. K. Dioumaev, R. Needleman, J. K. Lanyi, ibid. 75, 1455 (1998).
17. G. Véró and J. K. Lanyi, Biochemistry 30, 5016 (1991).
18. L. Zimányi et al., ibid. 31, 8535 (1992).
19. S. Subramaniam et al., J. Mol. Biol. 287, 145 (1999).
20. M. S. Braiman, O. Bousché, K. J. Rothschild, Proc. Natl. Acad. Sci. U.S.A. 88, 2388 (1991); B. Hessling, G. Souvignier, K. Gerwert, Biophys. J. 65, 1929 (1993).
21. M. S. Braiman, O. Bousché, K. J. Rothschild, Proc. Natl. Acad. Sci. U.S.A. 88, 2388 (1991); B. Hessling, G. Souvignier, K. Gerwert, Biophys. J. 65, 1929 (1993).
22. T. E. Thorgeirsson et al., J. Mol. Biol. 273, 951 (1997).
23. J. Sasaki, Y. Shichida, J. K. Lanyi, A. Maeda, J. Biol. Chem. 267, 20782 (1992).
24. C. Rödig and F. Siebert, FEBS Lett. 445, 14 (1999).
25. G. Rummel et al., J. Struct. Biol. 121, 82 (1998).
26. M. Kataoka et al., J. Mol. Biol. 243, 621 (1994).
27. B. Borucki, H. Otto, M. P. Heyn, J. Phys. Chem. B 102, 3821 (1998); T. N. Earnest, P. Roepe, M. S. Braiman, J. Gillespie, K. J. Rothschild, Biochemistry 25, 7793 (1986).
28. B. Borucki, H. Otto, M. P. Heyn, J. Phys. Chem. B 102, 3821 (1998); T. N. Earnest, P. Roepe, M. S. Braiman, J. Gillespie, K. J. Rothschild, Biochemistry 25, 7793 (1986).
29. S. Moltke et al., Biochemistry 37, 11821 (1998).
30. S. Subramaniam, D. A. Greenhalgh, P. Rath, K. J. Rothschild, H. G. Khorana, Proc. Natl. Acad. Sci. U.S.A. 88, 6873 (1991); H. Kandori et al., Biochemistry 36, 5134 (1997).
31. S. Subramaniam, D. A. Greenhalgh, P. Rath, K. J. Rothschild, H. G. Khorana, Proc. Natl. Acad. Sci. U.S.A. 88, 6873 (1991); H. Kandori et al., Biochemistry 36, 5134 (1997).
32. O. Weidlich et al., Biochemistry 35, 10807 (1996).
33. L. S. Brown and J. K. Lanyi, Proc. Natl. Acad. Sci. U.S.A. 93, 1731 (1996).
34. S. P. Balashov, E. S. Imasheva, R. Govindjee, T. G. Ebrey, Biophys. J. 70, 473 (1996); H.-T. Richter, L. S. Brown, R. Needleman, J. K. Lanyi, Biochemistry 35, 4054 (1996).
35. S. P. Balashov, E. S. Imasheva, R. Govindjee, T. G. Ebrey, Biophys. J. 70, 473 (1996); H.-T. Richter, L. S. Brown, R. Needleman, J. K. Lanyi, Biochemistry 35, 4054 (1996).
36. M. S. Braiman, A. K. Dioumaev, J. R. Lewis, Biophys. J. 70, 939 (1996).
37. G. Váró and J. K. Lanyi, ibid. 59, 313 (1991).
38. Y. Cao et al., Biochemistry 30, 10972 (1991).
39. H.J. Sass et al., EMBO J. 16, 1484 (1997); H. Kamikubo et al., Biochemistry 36, 12282 (1997).
40. H.J. Sass et al., EMBO J. 16, 1484 (1997); H. Kamikubo et al., Biochemistry 36, 12282 (1997).
41. M. Holz et al., Proc. Natl. Acad. Sci. U.S.A. 86, 2167 (1989); J. Tittor, C. Soell, D. Oesterhelt, H.-J. Butt, E. Bamberg, EMBO J. 8, 3477 (1989).
42. M. Holz et al., Proc. Natl. Acad. Sci. U.S.A. 86, 2167 (1989); J. Tittor, C. Soell, D. Oesterhelt, H.-J. Butt, E. Bamberg, EMBO J. 8, 3477 (1989).
43. A. K. Dioumaev, L. S. Brown, R. Needleman, J. K. Lanyi, Biochemistry 37, 9889 (1998).
44. K. Schulten and P. Tavan, Nature 272, 85 (1978); D. Oesterhelt, P. Hegemann, P. Tavan, K. Schulten, Eur. Biophys. J. 14, 123 (1986); K. Gerwert and F. Siebert, EMBO J. 5, 805 (1986).
45. K. Schulten and P. Tavan, Nature 272, 85 (1978); D. Oesterhelt, P. Hegemann, P. Tavan, K. Schulten, Eur. Biophys. J. 14, 123 (1986); K. Gerwert and F. Siebert, EMBO J. 5, 805 (1986).
46. K. Schulten and P. Tavan, Nature 272, 85 (1978); D. Oesterhelt, P. Hegemann, P. Tavan, K. Schulten, Eur. Biophys. J. 14, 123 (1986); K. Gerwert and F. Siebert, EMBO J. 5, 805 (1986).
47. L. S. Brown, A. K. Dioumaev, R. Needleman, J. K. Lanyi, Biochemistry 37, 3982 (1998).
48. C. Scharnagl, J. Hettenkofer, S. F. Fischer, J. Phys. Chem. 99, 7787 (1995).
49. L. S. Brown, G. Váró, R. Needleman, J. K. Lanyi, Biophys. J. 69, 2103 (1995).
50. Abbreviations for amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G. Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
51. R. Rammelsberg, G. Huhn, M. Lübben, K. Gerwert, Biochemistry 37, 5001 (1998).
52. Z. Otwinowski, in Data Collection and Processing, L. Sawyer, N. Isaacs, S. Bailey, Eds. (SERC Daresbury Laboratory, Warrington, U.K., 1993), p. 56.
53. G. M. Sheldrick and T. Schneider, Methods Enzymol. 277, 319 (1997).
54. Supported in part by grants from the National Institutes of Health to H.L. (R01-GM56445 and R01-GM59970) and J.K.L. (R01-GM29498) and from the Department of Energy to J.K.L. (DEFG03-86ER13525). The atomic coordinates of the BR and M states of the D96N mutant of bacteriorhodopsin have been deposited in the Protein Data Bank (accession numbers 1C8R and 1C8S, respectively).