Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor

Nature

Volumn 400, Issue 6746, 1999, Pages 787-792

  Kim, Kyeong Kyu ^a,b   Yokota, Hisao ^a   Kim, Sung Hou ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b Gyeongsang National University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE RECEPTOR;

ARTICLE; BACTERIAL MEMBRANE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

CHEMOTAXIS; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; CYTOPLASM; ESCHERICHIA COLI; METHYLATION; MODELS, MOLECULAR; MUTAGENESIS; PROTEIN CONFORMATION; RECEPTORS, AMINO ACID;

EID: 0001690764     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/23512     Document Type: Article

References (30)

1. Falke, J. J., Bass, R. B., Butler, S. L., Chervitz, S. A. & Danielson, M. A. The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymes. Annu. Rev. Cell Biol. Dev. Biol. 13, 457-512 (1997).
2. Ullrich, A. & Schlessinger, J. Signal transduction by receptors with tyrosine kinase activity. Cell 61, 203-212 (1990).
3. Chervitz, S. A. & Falke, J. J. Molecular mechanism of transmembrane signaling by the aspartate receptor: a model. Proc. Natl Acad. Sci. USA 93, 2545-2550 (1996).
4. Le Moual, H. & Koshland, D. E. Jr Molecular evolution of the C-terminal cytoplasmic domain of a superfamily of bacterial receptors involved in taxis. J. Mol. Biol. 261, 568-585 (1996).
5. Cochran, A. G. & Kim, P. S. Imitation of Escherichia coli aspartate receptor signaling in engineered dimers of the cytoplasmic domain. Science 271, 1113-1116 (1996).
6. Ames, P., Yu, Y. A. & Parkinson, J. S. Methylation segments are not required for chemotactic signalling by cytoplasmic fragments of Tsr, the methyl-accepting serine chemoreceptor of Escherichia coli. Mol. Microbiol. 19, 737-746 (1996).
7. Surette, M. G. & Stock, J. B. Role of α-helical coiled-coil interactions in receptor dimerization, signaling, and adaptation during bacterial chemotaxis. J. Biol. Chem. 271, 17966-17973 (1996).
8. Maddock, J. R. & Shapiro, L. Polar location of the chemoreceptor complex in the Escherichia coli cell. Science 259, 1717-1723 (1993).
9. Liu, Y., Levit, M., Lurz, R., Surette, M. G. & Stock, J. B. Receptor-mediated protein kinase activation and the mechanism of transmembrane signaling in bacterial chemotaxis. EMBO J. 16, 7231-7240 (1997).
10. Chi, Y. I., Yokota, H. & Kim, S.-H. Apo structure of the ligand-binding domain of aspartate receptor from Escherichia coli and its comparison with ligand-bound or pseudoligand-bound structures. FEBS Lett. 414, 327-332 (1997).
11. Lynch, B. A. & Koshland, D. E. Jr The fifth Datta Lecture. Structural similarities between the aspartate receptor of bacterial chemotaxis and the trp represser of E. coli. Implications for transmembrane signaling. FEBS Lett. 307, 3-9 (1992).
12. Gardina, P. J. & Manson, M. D. Attractant signaling by an aspartate chemoreceptor dimer with a single cytoplasmic domain. Science 274, 425-426 (1996).
13. Tatsuno, I., Homma, M., Oosawa, K. & Kawagishi, I. Signaling by the Escherichia coli aspartate chemoreceptor Tar with a single cytoplasmic domain per dimer. Science 274, 423-425 (1996).
14. Hughson, A. G. & Hazelbauer, G. L. Detecting the conformational change of transmembrane signaling in a bacterial chemoreceptor by measuring effects on disulfide cross-linking in vivo. Proc. Natl Acad. Sci. USA 93, 11546-11551 (1996).
15. Milburn, M. V. et al. Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand. Science 254, 1342-1347 (1991).
16. Kim, S.-H. "Frozen" dynamic dimer model for transmembrane signaling in bacterial chemotaxis receptors. Protein Sci. 3, 159-165 (1994).
17. Maruyama, I. N., Mikawa, Y. G. & Maruyama, H. I. A model for transmembrane signaling by the aspartate receptor based on random-cassette mutagenesis and site-directed disulfide cross-linking. J. Mol. Biol. 253, 530-546 (1995).
18. Borkovich, K. A., Alex, L. A. & Simon, M. I. Attenuation of sensory receptor signaling by covalent modification. Proc. Natl Acad. Sci. USA 89, 6756-6760 (1992).
19. Ames, P. & Parkinson, J. S. Transmembrane signaling by bacterial chemoreceptors: E. coli transducers with locked signal output. Cell 55, 817-826 (1988).
20. Ames, P., Chen, J., Wolff, C. & Parkinson, J. S. Structure-function studies of bacterial chemosensors. Cold Spring Harb. Symp. Quant. Biol. 53, 59-65 (1988).
21. Danielson, M. A., Bass, R. B. & Falke, J. J. Cysteine and disulfide scanning reveals a regulatory α-helix in the cytoplasmic domain of the aspartate receptor. J. Biol. Chem. 272, 32878-32888 (1997).
22. Bass, R. B. & Falke, J. J. Detection of a conserved α-helix in the kinase docking region of the aspartate receptor by cysteine and disulfide scanning. J. Biol. Chem. 273, 25006-25014 (1998).
23. Kunkel, T. A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl Acad. Sci. USA 82, 488 (1985).
24. Jancarik, J. & Kim, S.-H. Sparse matrix sampling: a screening method for crystallization of proteins. J. Appl. Crystallogr. 24, 409-411 (1991).
25. Otwinowski, Z. in Data Collection and Processing (eds Sawyer, L., Isaacs, N. & Bailey, S.) 56-62 (SERC Daresbury Laboratory, Warrington, UK, 1993).
26. Collaborative Computing Project No. 4. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
27. Jones, T. A., Zou, J.-Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for binding protein models inelectron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
28. Brünger, A. T. X-PLOR Version 3.1 (Yale Univ. Press, New Haven, CT, 1993).
29. Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thronton, J. M. Procheck: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
30. Kraulis, P. I. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).