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

Volumn 31, Issue 44, 1992, Pages 10657-10663

  Sharff, Andrew J ^a   Rodseth, Lynn E ^b   Spurlino, John C ^c   Quiocho, Florante A ^a  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

^b UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^c EASTMAN KODAK COMPANY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; LIGAND; MALTODEXTRIN;

ARTICLE; BINDING SITE; CELL MEMBRANE TRANSPORT; CHEMICAL BINDING; CHEMOTAXIS; CRYSTALLOGRAPHY; MEMBRANE BINDING; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BIOLOGICAL TRANSPORT, ACTIVE; CARRIER PROTEINS; CHEMOTAXIS; CRYSTALLIZATION; ESCHERICHIA COLI; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PROTEIN CONFORMATION; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; X-RAY DIFFRACTION;

ESCHERICHIA COLI;

EID: 0026493924     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi00159a003     Document Type: Article

References (51)

1. Anderson, B.F., Baker, H.M., Norris, G.E., Rumball, S.V., & Baker, E.N. (1990) Nature (London) 344, 784-787.
2. Bennett, W.S., & Huber, R. (1984) Crit. Rev. Biochem. 15, 291-384.
3. Brunger, A.T. (1990) X-PLOR, Version 2.1, Yale University, New Haven, CT.
4. Carson, M.C. (1987) J. Mol. Graphics 5, 103.
5. Dassa, E., & Hofnung, M. (1985) EMBO J. 4, 2287-2293.
6. Duplay, P., & Szmelcman, S. (1987) J. Mol. Biol. 194, 675-678.
7. Duplay, P., Szmelcman, S., Bedouelle, H., & Hofnung, M. (1987) J. Mol. Biol. 194, 663-673.
8. Falke, J.J., & Koshland, D.E., Jr. (1987) Science 237, 1596-1600.
9. Fitzgerald, P.M.D. (1988) J. Appl. Crystallogr. 21, 273-278.
10. Froshauer, S., & Beckwith, J. (1984) J. Biol. Chem. 259, 10896-10901.
11. Furlong, C.E. (1987) in Escherischia Coli and Salmonella typhimurium: Cellular and Molecular Biology (Neidhardt, F.C., Ingraham, J.L., Low, K.B., Magasanik, B., Schaechter, M., & Umbarger, H.E., Eds) pp 786-796, American Society for Microbiology, Washington, DC.
12. Gilson, E., Higgins, C.F., Hofnung, M., Ames, G.F.-L., & Nikaido, H. (1982) J. Biol. Chem. 257, 9915-9918.
13. Graham, H.C., Williams, R.J., Littlechild, J.A., & Watson, H.C. (1991) Eur. J., Biochem. 196, 261-269.
14. Hendrickson, W.A., & Konnert, J.H. (1980) in Computing in Crystallography, pp 13.01-13.23, Indian Academy ofScience, Bangalore.
15. Howard, A.J., Neilsen, C., & Xuong, N.H. (1985) Methods Enzymol. 114, 452-472.
16. Jacobson, B.L., He, J.J., Vermersch, P.S., Lemon, D.D., & Quiocho, F.A. (1991) J. Biol. Chem. 266, 5220-5225.
17. Jacobson, B.L., He, J.J., Lemon, D.D., & Quiocho, F.A. (1992) J. Mol. Biol. 223, 27-30.
18. Kang, C.-H., Shin, W.-C., Yamagata, Y., Gokeen, S., Ames, G.F., & Kim, S.-H. (1991) J. Biol. Chem. 266, 23893-23899.
19. Kossmann, M., Wolff, C., & Mason, M.D. (1988) J. Bacteriol. 170, 4516-4521.
20. Luck, L.A.F.J. (1991 a) Biochemistry 30, 4248-4256.
21. Luck, L.A., & Falke, J.J. (1991 b) Biochemistry 30, 4257-4261.
22. Luecke, H., & Quiocho, F.A. (1990) Nature (London) 347, 402-406.
23. Macnab, R. (1987) in Escherischia coli and Salmonella typhimurium Cellular and Molecular Biology (Neidhardt, F.C., Ingraham, J.L., Low, K.B., Magasanik, B., Schaechter, M., & Umbarger, H.E., Eds.) pp 732-759, American Society for Microbiology, Washington, DC.
24. Mao, B., Pear, M.R., McCammon, J.A., & Quiocho, F.A. (1982) J. Biol. Chem. 257, 1131-1133.
25. Martineau, P., Saurin, W., Hofnung, M., Spurlino, J.C., & Quiocho, F.A. (1990) Biochimie 72, 397-402.
26. Milburn, M.W., Privé, G.G., Milligan, D.L., Scott, W.G., Yeh, J., Jancarik, J., Koshland, D.E., Jr., & Kim, S.-H. (1991) Science 254, 1342-1347.
27. Miller, D.M.I., Olson, J.S., Pflugrath, J.W., & Quiocho, F.A. (1983) J. Biol. Chem. 258, 13665-13672.
28. Mowbray, S.L., & Cole, L.B. (1992) J. Mol. Biol. 225, 155-175.
29. Mowbray, S.L., Smith, R.D., & Cole, L.B. (1990) Receptor I, 41-45.
30. Newcomer, M.E., Lewis, B.A., & Quiocho, F.A. (1981) J. Biol. Chem. 256, 13218-13222.
31. Pfugrath, J.W., & Quiocho, F.A. (1985) Nature (London) 314, 257-260.
32. Pfugrath, J.W., & Quiocho, F.A. (1988) J. Mol. Biol. 200, 163-180.
33. Quiocho, F.A. (1990) Philos. Trans. R., Soc. London 326, 341-351.
34. Quiocho, F.A., & Vyas, N.K. (1984) Nature (London) 310, 381-386.
35. Quiocho, F.A., Gilliland, G.L., & Phillips, G.N., Jr. (1977) J. Biol. Chem. 252, 5142-5149.
36. Rossmann, M.G., & Argos, P. (1977) J. Mol. Biol. 109, 99-129.
37. Sack, J.S. (1988) J. Mol. Graphics 6, 244-245.
38. Sack, J.S., Saper, M.A., & Quiocho, F.A. (1989 a) J. Mol. Biol. 206, 171-191.
39. Sack, J.S., Trakhanov, S.D., Tsigannik, I.H., & Quiocho, F.A. (1989 b) J. Mol. Biol. 206, 193-207.
40. Spurlino, J.C., Lu, G.-Y., & Quiocho, F.A. (1991) J. Biol. Chem. 266, 5202-5219.
41. Steitz, T.A., Fletterick, R.J., Anderson, W.F., & Anderson, C.M. (1976) J. Mol. Biol. 104, 197.
42. Treptow, N.A., & Shuman, H.A. (1985) J. Bacteriol. 163, 654-660.
43. Treptow, N.A., & Shuman, H.A. (1988) J. Mol. Biol. 202, 809-822.
44. Vermersch, P.S., Tesmer, J.J., Lemon, D.L., & Quiocho, F.A. (1990) J. Biol. Chem. 265, 16592-16603.
45. Vermersch, P.S., Lemon, D.D., Tesmer, J.J., & Quiocho, F.A. (1991) Biochemistry 30, 6861-6866.
46. Vyas, N.K., Vyas, M.N., & Quiocho, F.A. (1987) Nature (London) 327, 635-638.
47. Vyas, N.K., Vyas, M.N., & Quiocho, F.A. (1988) Science 242, 1290-1295.
48. Vyas, N.K., Vyas, M.N., & Quiocho, F.A. (1991) J. Biol. Chem. 266, 5226-5237.
49. Walmsley, A.R., Shaw, J.G., & Kelly, D.J. (1992) J. Biol. Chem. 267, 8064-8072.
50. Xuong, N.H., Nielsen, C., Hamlin, R., & Anderson, D. (1985) J. Appl. Crystallogr. 18, 342-350.
51. Zhang, Y., Conway, C., Rosato, M., Suh, Y., & Manson, M.D. (1992) J. Biol. Chem. (in press).