Apo structure of the ligand-binding domain of aspartate receptor from Escherichia coli and its comparison with ligand-bound or pseudoligand-bound structures

FEBS Letters

Volumn 414, Issue 2, 1997, Pages 327-332

  Chi, Young In ^a   Yokota, Hisao ^a   Kim, Sung Hou ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Aspartate receptor; Chemotaxis; Crystal structure; Transmembrane signaling; X ray crystallogrpahy

Indexed keywords

AMINO ACID RECEPTOR;

ARTICLE; BINDING SITE; CHEMOTAXIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ESCHERICHIA COLI; LIGAND BINDING; PRIORITY JOURNAL; RECEPTOR BINDING; SIGNAL TRANSDUCTION;

APOPROTEINS; ASPARTIC ACID; BINDING SITES; CELL MEMBRANE; CHEMOTAXIS; COMPUTER SIMULATION; CRYSTALLOGRAPHY; DIMERIZATION; ESCHERICHIA COLI; LIGANDS; MODELS, MOLECULAR; MODELS, STRUCTURAL; PROTEIN CONFORMATION; RECEPTORS, AMINO ACID; SIGNAL TRANSDUCTION; SOFTWARE; STRUCTURE-ACTIVITY RELATIONSHIP;

ESCHERICHIA COLI;

EID: 0031559942     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(97)01027-2     Document Type: Article

References (29)

1. [1] Milburn, M., Prive, G., Milligan, D., Scott, W., Yeh, J., Jancarik, J., Koshland Jr., D.E. and Kim, S.-H. (1991) Science 254, 1342-1347.
2. [2] Yeh, J., Biemann, H.-P., Pandit, J., Koshland Jr., D.E. and Kim, S.-H. (1993) J. Biol. Chem. 268, 9787-9792.
3. [3] Scott, W., Milligan, D., Milburn, M., Prive, G., Yeh, J., Koshland Jr., D.E. and Kim, S.-H. (1993) J. Mol. Biol. 232, 555-573.
4. [4] Bowie, J.U., Pakula, A.A. and Simon, W.I. (1995) Acta Cryst. D51, 145-154.
5. [5] de Vos, A.M., Ultsch, M. and Kossiakoff, A.A. (1992) Science 255, 306-312.
6. [6] Milligan, D.L. and Koshland Jr., D.E. (1988) J. Biol. Chem. 263, 6268-6275.
7. [7] Falke, J.J. and Koshland Jr., D.E. (1987) Science 237, 1596-1600.
8. [8] Milligan, D.L. and Koshland Jr., D.E. (1991) Science 254, 1651-1654.
9. [9] Hughson, A.G. and Hazelbauer, G.L. (1996) Proc. Natl. Acad. Sci. USA 93, 11546-11551.
10. [10] Tatsuno, I., Homma, M., Oosawa, K. and Kawagishi, I. (1996) Science 274, 423-425.
11. [11] Gardina, P.J. and Manson, M.D. (1996) Science 274, 425-426.
12. [12] Lynch, B.A. and Koshland Jr., D.E. (1992) FEBS Lett. 307, 3-9.
13. [13] Kim, S.-H. (1994) Protein Sci. 3, 159-165.
14. [14] Jancarik, J., Scott, W.G., Milligan, D.L., Koshland Jr., D.E. and Kim, S.-H. (1991) J. Mol. Biol. 221, 31-34.
15. [15] Jancarik, J. and Kim, S.-H. (1991) J. Appl. Crystallogr. 24, 409-411.
16. [16] Ozwinowsk, Z. (1993) in Data Collection and Processing, Sawyer, L., Isaacs, N., Bailey, S. Eds. (SERC Darsberry Laboratory, Warrington, UK) pp. 56-62.
17. [17] CCP4: Collaborative Computational Project No. 4. Daresbury, UK (1994) Acta Cryst. D50, 760-763.
18. [18] Navazo, J. (1994) Acta Cryst. A50, 157-163.
19. [19] Brünger, A.T. (1992) X-PLOR manual version 3.1 (Yale University, New Haven, CT).
20. [20] Brünger, A.T. (1992) Nature 355, 472-475.
21. [21] Jones, T.A., Zou, J.-Y., Cowan, S.W. and Kjeldgaard, M. (1991) Acta Cryst. A47, 110-119.
22. [22] Danielson, M.A., Biemann, H.P., Koshland Jr., D.E. and Falkem, J.J. (1994) Biochemistry 33, 6100-6109.
23. [23] Cochran, A.G. and Kim, P.S. (1996) Science 271, 1113-1116.
24. [24] Surette, M.G. and Stock, J.B. (1996) J. Biol. Chem. 271, 17966-17973.
25. [25] Maruyama, I.N., Mikawa, Y.G. and Maruyama, H.I. (1995) J. Mol. Biol. 253, 530-546.
26. [26] Chervitz, S.A. and Falke, J.J. (1996) Proc. Natl. Acad. Sci. USA 93, 2545-2550.
27. [27] Scott, W.G. and Stoddard, B.L. (1994) Structure 2, 877-887.
28. [28] Zhang, R.-G., Joachimiak, A., Lawson, C.L., Schevitz, R.W., Otwinowski, Z. and Sigler, P.B. (1987) Nature 327, 591-597.
29. [29] Schevitz, R.W., Otwinowski, Z., Joachimiak, A., Lawson, C.L. and Sigler, P.B. (1985) Nature 317, 782-786.