Aspartate Receptors of Escherichia coli and Salmonella typhimurium Bind Ligand with Negative and Half-of-the-Sites Cooperativity

Biochemistry

Volumn 33, Issue 3, 1994, Pages 629-634

  Biemann, Hans Peter ^a   Koshland, Daniel E ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ARGININE; ASPARTIC ACID; CYSTEINE; MEMBRANE PROTEIN; MEMBRANE RECEPTOR; SERINE; TYROSINE;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; CROSS LINKING; CRYSTAL STRUCTURE; DISULFIDE BOND; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; RECEPTOR BINDING; SALMONELLA TYPHIMURIUM; SCATCHARD PLOT; STOICHIOMETRY; X RAY CRYSTALLOGRAPHY;

ALLOSTERIC REGULATION; ASPARTIC ACID; COMPARATIVE STUDY; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; KINETICS; LIGANDS; MODELS, MOLECULAR; PROTEIN CONFORMATION; RECEPTORS, AMINO ACID; SALMONELLA TYPHIMURIUM; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.;

EID: 0028089151     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi00169a002     Document Type: Article

References (24)

1. Benton, H. P. (1991) Curr. Opin. Cell Biol. 3, 171–175.
2. Borkovich, K. A., Alex, L. A., & Simon, M. I. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 6756–6760.
3. Clarke, S., & Koshland, D. E., Jr. (1979) J. Biol. Chem. 254, 9695–9702.
4. Dunten, P., & Koshland, D. E., Jr. (1991) J. Biol. Chem. 266, 1491–1496.
5. Eisenstein, E., Markby, D. W., & Schachman, H. K. (1990) Biochemistry 29, 3724–3731.
6. Falke, J. J., & Koshland, D. E., Jr. (1987) Science 237, 1596–1600.
7. Foster, D. L., Mowbray, S. L., Jap, B. K., & Koshland, D. E., Jr. (1985) J. Biol. Chem. 260, 11706–11710.
8. Hill, A. V. (1913) Biochem. J. 7, 471.
9. Koshland, D. E., Jr., Némethy, G., & Filmer, D. (1966) Biochemistry 5, 365–385.
10. Krikos, A., Mutoh, N., Boyd, A., & Simon, M. I. (1983) Cell 33, 615–622.
11. Levitzki, A., & Koshland, D. E., Jr. (1969) FEBS Symp. 19, 263–270.
12. Long, C. W., Levitzki, A., & Koshland, D. E., Jr. (1970) J. Biol. Chem. 245, 80–87.
13. Lynch, B. A., & Koshland, D. E., Jr. (1992) FEBS Lett. 307, 3–9.
14. Milburn, M. V., Privé, G. G., Mulligan, D. L., Scott, W. G., Yeh, J., Jancarik, J., Koshland, D. E., Jr., & Kim, S.-H. (1991) Science 254, 1342–1347.
15. Milligan, D., & Koshland, D. E., Jr. (1993) J. Biol. Chem. 268, 19991–19997.
16. Mowbray, S. L., & Koshland, D. E., Jr. (1987) Cell 50, 171–180.
17. Mowbray, S. L., Foster, D. L., & Koshland, D. E., Jr. (1985) J. Biol. Chem. 260, 11711–11718.
18. Russo, A. F., & Koshland, D. E., Jr. (1983) Science 220, 1016–1020.
19. Scatchard, G. (1949) Ann. N.Y. Acad. Sci. 51, 660–672.
20. Scrutton, N. S., Deonarain, M. P., Berry, A., & Perham, R. N. (1992) Science 258, 1140–1142.
21. Stoddard, B. L., & Koshland, D. E., Jr. (1992) Nature 358, 774–776.
22. Stoddard, B. L., Biemann, H.-P., & Koshland, D. E., Jr. (1992) Cold Spring Harbor Symp. Quant. Biol. 57, 1–15.
23. Wang, E. A., & Koshland, D. E., Jr. (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 7157–7161.
24. Yeh, J. I., Biemann, H.-P., Pandit, J., Koshland, D. E., Jr., & Kim, S.-H. (1993) J. Biol. Chem. 268, 9787–9782.