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Volumn 262, Issue 2, 1996, Pages 186-201

High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor

Author keywords

Aspartate receptor structure; Conformational changes; Receptor ligand interactions; Transmembrane signaling; X ray crystal structure

Indexed keywords

ASPARTIC ACID; BACTERIAL PROTEIN; PROTEIN SUBUNIT; RECEPTOR; SULFATE; WATER;

EID: 0030595334     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0507     Document Type: Article
Times cited : (142)

References (40)
  • 1
    • 0014692237 scopus 로고
    • Chemotaxis in bacteria
    • Adler, J. (1969). Chemotaxis in bacteria. Science, 166, 1588-1597.
    • (1969) Science , vol.166 , pp. 1588-1597
    • Adler, J.1
  • 2
    • 0028089151 scopus 로고
    • Aspartate receptors of Escherichia coli and Salmonella typhimurium bind ligand with negative and half-of-the-sites cooperativity
    • Biemann, H.-P. & Koshland, D. E., Jr (1994). Aspartate receptors of Escherichia coli and Salmonella typhimurium bind ligand with negative and half-of-the-sites cooperativity. Biochemistry, 33, 629-634.
    • (1994) Biochemistry , vol.33 , pp. 629-634
    • Biemann, H.-P.1    Koshland D.E., Jr.2
  • 3
    • 0021238169 scopus 로고
    • Structure of the trg protein: Homologies with and differences from other sensory transducers of Escherichia coli
    • Bollinger, J., Park, C., Harayama, S. & Hazelbauer, G. L. (1984). Structure of the trg protein: homologies with and differences from other sensory transducers of Escherichia coli. Proc. Natl Acad. Sci. USA, 81, 3287-3291.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 3287-3291
    • Bollinger, J.1    Park, C.2    Harayama, S.3    Hazelbauer, G.L.4
  • 4
    • 0029108209 scopus 로고
    • The three-dimensional structure of the aspartate receptor from Escherichia coli
    • Bowie, J. U., Pakula, A. A. & Simon, M. I. (1995). The three-dimensional structure of the aspartate receptor from Escherichia coli. Acta Crystallog. sect. D, 51, 145-154.
    • (1995) Acta Crystallog. Sect. D , vol.51 , pp. 145-154
    • Bowie, J.U.1    Pakula, A.A.2    Simon, M.I.3
  • 5
    • 0020693765 scopus 로고
    • Structure of the serine chemoreceptor in Escherichia coli
    • Boyd, A., Kendall, K. & Simon, M. I. (1983). Structure of the serine chemoreceptor in Escherichia coli. Nature, 301, 623-626.
    • (1983) Nature , vol.301 , pp. 623-626
    • Boyd, A.1    Kendall, K.2    Simon, M.I.3
  • 6
    • 84944812221 scopus 로고
    • Extension of molecular replacement: A new search strategy based on Patterson correlation refinement
    • Brünger, A. T. (1990). Extension of molecular replacement: a new search strategy based on Patterson correlation refinement. Acta Crystallog. sect. A, 46, 46-57.
    • (1990) Acta Crystallog. Sect. A , vol.46 , pp. 46-57
    • Brünger, A.T.1
  • 7
    • 0018712142 scopus 로고
    • Membrane receptors for aspartic and serine in bacterial chemotaxis
    • Clarke, S. & Koshland, D. E., Jr (1979). Membrane receptors for aspartic and serine in bacterial chemotaxis. J. Biol. Chem. 254, 9695-9702.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9695-9702
    • Clarke, S.1    Koshland D.E., Jr.2
  • 9
    • 0026521574 scopus 로고
    • Aspartate and maltose-binding protein interact with adjacent sites in the Tar chemotactic signal transduction in Escherichia coli
    • Gardina, P., Conway, C., Kossman, M. & Manson, M. (1992). Aspartate and maltose-binding protein interact with adjacent sites in the Tar chemotactic signal transduction in Escherichia coli. J. Bacteriol. 174, 1528-1236.
    • (1992) J. Bacteriol. , vol.174 , pp. 1528-11236
    • Gardina, P.1    Conway, C.2    Kossman, M.3    Manson, M.4
  • 11
    • 0021057460 scopus 로고
    • Chemotactic response of Escherichia coli to chemically synthesized amino acids
    • Hedblom, M. L. & Adler, J. (1983). Chemotactic response of Escherichia coli to chemically synthesized amino acids. J. Bacteriol. 155, 1463-1466.
    • (1983) J. Bacteriol. , vol.155 , pp. 1463-1466
    • Hedblom, M.L.1    Adler, J.2
  • 12
    • 0000933280 scopus 로고
    • Transformations to optimize the superposition of similar structures
    • Hendrickson, W. A. (1979). Transformations to optimize the superposition of similar structures. Acta Crystallog. sect. A, 35, 158-163.
    • (1979) Acta Crystallog. Sect. A , vol.35 , pp. 158-163
    • Hendrickson, W.A.1
  • 13
    • 0028294190 scopus 로고
    • A single hydrophobic to hydrophobic substitution in the transmembrane domain impairs aspartate receptor function
    • Jeffrey, C. J. & Koshland, D. E., Jr (1993). A single hydrophobic to hydrophobic substitution in the transmembrane domain impairs aspartate receptor function. Biochemistry, 33, 3457-3463.
    • (1993) Biochemistry , vol.33 , pp. 3457-3463
    • Jeffrey, C.J.1    Koshland D.E., Jr.2
  • 14
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch, W. (1976). A solution for the best rotation to relate two sets of vectors. Acta Crystallog. 32, 922-923.
    • (1976) Acta Crystallog. , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 16
    • 0028175609 scopus 로고
    • "Frozen" dynamic dimer model for transmembrane signaling in bacterial chemotaxis receptors
    • Kim, S.-H. (1994). "Frozen" dynamic dimer model for transmembrane signaling in bacterial chemotaxis receptors. Protein Sci. 3, 159-165.
    • (1994) Protein Sci. , vol.3 , pp. 159-165
    • Kim, S.-H.1
  • 17
    • 0019365819 scopus 로고
    • Biochemistry of sensing and adaptation in a simple bacterial system
    • Koshland, D. E., Jr (1981). Biochemistry of sensing and adaptation in a simple bacterial system. Annu. Rev. Biochem. 50, 765-782.
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 765-782
    • Koshland D.E., Jr.1
  • 18
    • 0020771141 scopus 로고
    • Sensory transducers of E. coli are composed of discrete structural and functional domains
    • Krikos, A., Mutoh, N., Boyd, A. & Simon, M. I. (1983). Sensory transducers of E. coli are composed of discrete structural and functional domains. Cell, 33, 615-622.
    • (1983) Cell , vol.33 , pp. 615-622
    • Krikos, A.1    Mutoh, N.2    Boyd, A.3    Simon, M.I.4
  • 19
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B. & Richards, F. M. (1971). The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55, 379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 20
    • 0028924963 scopus 로고
    • Transmembrane signaling characterized in bacterial chemoreceptors by using sulfhydryl cross-linking in vivo
    • Lee, G. F., Lebert, M. R., Lilly, A. A. & Hazelbauer, G. L. (1995). Transmembrane signaling characterized in bacterial chemoreceptors by using sulfhydryl cross-linking in vivo. Proc. Natl Acad. Sci. USA, 92, 3391-3395.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3391-3395
    • Lee, G.F.1    Lebert, M.R.2    Lilly, A.A.3    Hazelbauer, G.L.4
  • 21
    • 0025058595 scopus 로고
    • Role of threonine residue 154 in ligand recognition of the Tar chemoreceptor in Escherichia coli
    • Lee, L. & Imae, Y. (1990). Role of threonine residue 154 in ligand recognition of the Tar chemoreceptor in Escherichia coli. J. Bacteriol. 172, 377-382.
    • (1990) J. Bacteriol. , vol.172 , pp. 377-382
    • Lee, L.1    Imae, Y.2
  • 22
    • 0025872118 scopus 로고
    • Disulfide cross-linking studies of the transmembrane regions of the aspartate receptor of Escherichia coli
    • Lynch, B. A. & Koshland, D. E., Jr (1991). Disulfide cross-linking studies of the transmembrane regions of the aspartate receptor of Escherichia coli. Proc. Natl Acad. Sci. USA, 88, 10402-10406.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 10402-10406
    • Lynch, B.A.1    Koshland D.E., Jr.2
  • 23
    • 0015397646 scopus 로고
    • The gradient-sensing mechanism in bacterial chemotaxis
    • Macnab, R. M. & Koshland, D. E., Jr (1972). The gradient-sensing mechanism in bacterial chemotaxis. Proc. Natl Acad. Sci. USA, 69, 2509-2512.
    • (1972) Proc. Natl Acad. Sci. USA , vol.69 , pp. 2509-2512
    • Macnab, R.M.1    Koshland D.E., Jr.2
  • 24
    • 0026315513 scopus 로고
    • Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand
    • Milburn, M. V., Prive, G. G., Milligan, D. L., Scott, W. G., Yeh, J., Jancarik, J., Koshland, D. E. & Kim, S.-H. (1991). Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand. Science, 254, 1342-1347.
    • (1991) Science , vol.254 , pp. 1342-1347
    • Milburn, M.V.1    Prive, G.G.2    Milligan, D.L.3    Scott, W.G.4    Yeh, J.5    Jancarik, J.6    Koshland, D.E.7    Kim, S.-H.8
  • 25
    • 0026342828 scopus 로고
    • Intra-subunit signal transduction by the aspartate chemoreceptor
    • Milligan, D. L. & Koshland, D. E., Jr (1991). Intra-subunit signal transduction by the aspartate chemoreceptor. Science, 254, 1651-1654.
    • (1991) Science , vol.254 , pp. 1651-1654
    • Milligan, D.L.1    Koshland D.E., Jr.2
  • 26
    • 0027248998 scopus 로고
    • Purification and characterization of the periplasmic domain of the aspartate chemoreceptor
    • Milligan, D. L. & Koshland, D. E., Jr (1993). Purification and characterization of the periplasmic domain of the aspartate chemoreceptor. J. Biol. Chem. 268, 19991-19997.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19991-19997
    • Milligan, D.L.1    Koshland D.E., Jr.2
  • 27
    • 0023658327 scopus 로고
    • Additive and independent responses in a single receptor: Aspartate and maltose stimuli on the Tar protein
    • Mowbray, S. L. & Koshland, D. E., Jr (1987). Additive and independent responses in a single receptor: aspartate and maltose stimuli on the Tar protein. Cell, 50, 171-180.
    • (1987) Cell , vol.50 , pp. 171-180
    • Mowbray, S.L.1    Koshland D.E., Jr.2
  • 28
    • 0025150830 scopus 로고
    • Mutations in the aspartate receptor which affects aspartate binding
    • Mowbray, S. L. & Koshland, D. E., Jr (1990). Mutations in the aspartate receptor which affects aspartate binding. J. Biol. Chem. 265, 15638-15643.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15638-15643
    • Mowbray, S.L.1    Koshland D.E., Jr.2
  • 30
    • 0026605299 scopus 로고
    • Determination of transmembrane protein structure by disulfide cross-linking: The Escherichia coli Tar receptor
    • Pakula, A. A. & Simon, M. I. (1992). Determination of transmembrane protein structure by disulfide cross-linking: the Escherichia coli Tar receptor. Proc. Natl Acad. Sci. USA, 89, 10402-10406.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10402-10406
    • Pakula, A.A.1    Simon, M.I.2
  • 31
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R. J. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallog. sect. A, 42, 140-149.
    • (1986) Acta Crystallog. Sect. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 32
    • 0027295669 scopus 로고
    • Refined structures of the ligand binding domain of the aspartate receptor from Salmonella typhimurium
    • Scott, W. G., Milligan, D. L., Milburn, M. V., Prive, G. G., Yeh, J. I., Koshland, D. E. & Kim, S.-H. (1993). Refined structures of the ligand binding domain of the aspartate receptor from Salmonella typhimurium. J. Mol. Biol. 232, 555-573.
    • (1993) J. Mol. Biol. , vol.232 , pp. 555-573
    • Scott, W.G.1    Milligan, D.L.2    Milburn, M.V.3    Prive, G.G.4    Yeh, J.I.5    Koshland, D.E.6    Kim, S.-H.7
  • 33
    • 0016351193 scopus 로고
    • Flagellar rotation and the mechanism of bacterial motility
    • Silverman, M. & Simon, M. (1974). Flagellar rotation and the mechanism of bacterial motility. Nature, 249, 73-74.
    • (1974) Nature , vol.249 , pp. 73-74
    • Silverman, M.1    Simon, M.2
  • 34
    • 0017333058 scopus 로고
    • Sensory transduction in Escherichia coli: A requirement for methionine in sensory adaptation
    • Springer, M. S., Goy, M. F. & Adler, J. (1977). Sensory transduction in Escherichia coli: a requirement for methionine in sensory adaptation. Proc. Natl Acad. Sci. USA, 74, 183-187.
    • (1977) Proc. Natl Acad. Sci. USA , vol.74 , pp. 183-187
    • Springer, M.S.1    Goy, M.F.2    Adler, J.3
  • 35
    • 0028774184 scopus 로고
    • transmembrane signalling and the aspartate receptor
    • Stoddard, B. L. & Scott, W. G. (1994). transmembrane signalling and the aspartate receptor. Structure, 2, 877-888.
    • (1994) Structure , vol.2 , pp. 877-888
    • Stoddard, B.L.1    Scott, W.G.2
  • 37
    • 0019174856 scopus 로고
    • Receptor structure in the bacterial sensing system
    • Wang, E. & Koshland, D. E., Jr (1980). Receptor structure in the bacterial sensing system. Proc. Natl Acad. Sci. USA, 77, 7157-7161.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 7157-7161
    • Wang, E.1    Koshland D.E., Jr.2
  • 38
    • 0024093975 scopus 로고
    • Aspartate taxis mutants of Escherichia coli Tar chemoreceptor
    • Wolff, C. & Parkinson, J. S. (1988). Aspartate taxis mutants of Escherichia coli Tar chemoreceptor. J. Bacteriol. 170, 4509-4515.
    • (1988) J. Bacteriol. , vol.170 , pp. 4509-4515
    • Wolff, C.1    Parkinson, J.S.2
  • 39
    • 0027397908 scopus 로고
    • Cloning and characterization of the Salmonella typhimurium specific chemoreceptor Tcp for taxis to citrate and from phenol
    • Yamamoto, K. & Imae, Y. (1993). Cloning and characterization of the Salmonella typhimurium specific chemoreceptor Tcp for taxis to citrate and from phenol. Proc. Natl Acad. Sci. USA, 90, 217-221.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 217-221
    • Yamamoto, K.1    Imae, Y.2
  • 40
    • 0027175202 scopus 로고
    • The three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis receptor
    • Yeh, J. I., Biemann, H.-P., Pandit, J., Koshland, D. E., Jr & Kim, S.-H. (1993). The three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis receptor. J. Biol. Chem. 268, 9787-9792.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9787-9792
    • Yeh, J.I.1    Biemann, H.-P.2    Pandit, J.3    Koshland D.E., Jr.4    Kim, S.-H.5


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