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Volumn 274, Issue 5288, 1996, Pages 761-765

The crystal structure of a five-stranded coiled coil in COMP: A prototype ion channel?

Author keywords

[No Author keywords available]

Indexed keywords

CHOLINERGIC RECEPTOR; DISULFIDE; GLUTAMINE; ION CHANNEL; MATRIX PROTEIN; PHOSPHOLAMBAN; SCLEROPROTEIN; THROMBOSPONDIN;

EID: 0029911261     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.274.5288.761     Document Type: Article
Times cited : (285)

References (37)
  • 2
    • 0027934571 scopus 로고
    • P. B. Harbury, T. Zhang, P. S. Kim, T. Alber, Science 262, 1401 (1993); P. B. Harbury, P. S. Kim, T. Alber, Nature 371,80 (1994).
    • (1994) Nature , vol.371 , pp. 80
    • Harbury, P.B.1    Kim, P.S.2    Alber, T.3
  • 3
    • 0026703257 scopus 로고
    • M. Mörgelin, D. Heinegård. J. Engel, M. Paulsson, J. Biol. Chem. 267, 6137 (1992); P. E. DiCesare, M. Mörgelin, K. Mann, M. Paulsson, Eur. J. Biochem. 223,927 (1994); G. Newton et al., Genomics 24, 435 (1994).
    • (1992) J. Biol. Chem. , vol.267 , pp. 6137
    • Mörgelin, M.1    Heinegård, D.2    Engel, J.3    Paulsson, M.4
  • 4
  • 5
    • 0028601305 scopus 로고
    • M. Mörgelin, D. Heinegård. J. Engel, M. Paulsson, J. Biol. Chem. 267, 6137 (1992); P. E. DiCesare, M. Mörgelin, K. Mann, M. Paulsson, Eur. J. Biochem. 223,927 (1994); G. Newton et al., Genomics 24, 435 (1994).
    • (1994) Genomics , vol.24 , pp. 435
    • Newton, G.1
  • 6
    • 0029070839 scopus 로고
    • A. Qabar, L. Derick, J. Lawler, V. Dixit, J. Biol. Chem. 270, 12725 (1995); N. Hauser, M. Paulsson, A. A. Kale, P. E. DiCesare, FEBS Lett. 368, 307 (1995); J. Lawler, K. McHenry, M. Duquette, L. Derick, J. Biol. Chem. 270, 2809 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 12725
    • Qabar, A.1    Derick, L.2    Lawler, J.3    Dixit, V.4
  • 7
    • 0029055720 scopus 로고
    • A. Qabar, L. Derick, J. Lawler, V. Dixit, J. Biol. Chem. 270, 12725 (1995); N. Hauser, M. Paulsson, A. A. Kale, P. E. DiCesare, FEBS Lett. 368, 307 (1995); J. Lawler, K. McHenry, M. Duquette, L. Derick, J. Biol. Chem. 270, 2809 (1995).
    • (1995) FEBS Lett. , vol.368 , pp. 307
    • Hauser, N.1    Paulsson, M.2    Kale, A.A.3    DiCesare, P.E.4
  • 8
    • 0028833511 scopus 로고
    • A. Qabar, L. Derick, J. Lawler, V. Dixit, J. Biol. Chem. 270, 12725 (1995); N. Hauser, M. Paulsson, A. A. Kale, P. E. DiCesare, FEBS Lett. 368, 307 (1995); J. Lawler, K. McHenry, M. Duquette, L. Derick, J. Biol. Chem. 270, 2809 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 2809
    • Lawler, J.1    McHenry, K.2    Duquette, M.3    Derick, L.4
  • 13
    • 10544240871 scopus 로고    scopus 로고
    • unpublished results
    • R. A. Kammerer, unpublished results.
    • Kammerer, R.A.1
  • 14
    • 10544221345 scopus 로고    scopus 로고
    • note
    • m = 45° ± 1 °C) indicates that although ionic interactions do play a moderate role in stabilizing the structure of the pentameric bundle, they may be especially important in guiding the correct assembly of the helices.
  • 15
    • 10544242664 scopus 로고    scopus 로고
    • note
    • 2 per residue). This results from the larger axial pore diameter in COMP, which makes residues at positions a and d more accessible to water molecules, whereas in the tetramer (1), water is excluded by the small channel radius of 1.0 to 1.3 Å. Water in the narrow pentameric channel cannot form clathrate cages around hydrophobic groups, as it does in bulk solvent (18). The resulting entropy gain may explain why a pore of the size found in the COMP pentamer does not destabilize the structure. Larger hydrophobic pores would be entropy-opposed, making hexameric or larger coiled-coil structures less probable.
  • 16
    • 10544256305 scopus 로고    scopus 로고
    • note
    • - is the most likely anion, because crystalization was performed in the presance 0.5 M NaCl.
  • 18
    • 0029051933 scopus 로고
    • I. T. Arkin et al., J. Mol. Biol. 248, 824 (1995); I. T. Arkin et al., EMBO J. 13, 4757 (1994).
    • (1995) J. Mol. Biol. , vol.248 , pp. 824
    • Arkin, I.T.1
  • 19
    • 0028063482 scopus 로고
    • I. T. Arkin et al., J. Mol. Biol. 248, 824 (1995); I. T. Arkin et al., EMBO J. 13, 4757 (1994).
    • (1994) EMBO J. , vol.13 , pp. 4757
    • Arkin, I.T.1
  • 23
    • 0029163027 scopus 로고    scopus 로고
    • M. A. Lester, Annu. Rev. Biophys. Biomol. Struct. 21, 267 (1992); C. Labarca et al., Nature 376, 514 (1996).
    • (1996) Nature , vol.376 , pp. 514
    • Labarca, C.1
  • 24
    • 0028921479 scopus 로고
    • N.Unwin, Nature 373, 37 (1995).
    • (1995) Nature , vol.373 , pp. 37
    • Unwin, N.1
  • 25
    • 0003516749 scopus 로고
    • Oxford Univ. Press, New York ed. 5
    • P. W. Atkins, Physical Chemistry (Oxford Univ. Press, New York ed. 5, 1994).
    • (1994) Physical Chemistry
    • Atkins, P.W.1
  • 26
    • 0004148514 scopus 로고
    • Medical Research Council, Laboratory of Molecular Biology, Cambrige
    • A. G. V. Leslie, MOSFLM Users Guide (Medical Research Council, Laboratory of Molecular Biology, Cambrige, 1994).
    • (1994) MOSFLM Users Guide
    • Leslie, A.G.V.1
  • 27
    • 0028103275 scopus 로고
    • Coliaborative Computing Project Number 4, Acta Crystallogr. D 50, 760 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760
  • 28
    • 10544229067 scopus 로고    scopus 로고
    • note
    • 66 (M66A) mutant to decrease the number of heavy atoms in the asymmetric unit and to Obtain an additional derfivative. Several diffraction data sets were cofected in the laboratory, as described above, and others were Collected on the BW7B beamiine at the Eurpean Molecular Biology Laboratory outstation, Hamburg, Germany (λ = 0.882 Å) and on the Swiss Norwegian beamline at the European synchroton Radiation Facility, Grenoble, France (λ = 0.875Å). Although an amino acid analysis indicated that selenomethionine was successfully incorporated in both wild-type and M66A COMP, we were not able to detect any signal from the Se atoms, using either isomorphous difference or anomalous Patterson techniques. We continued the search for heavy atom derivatives, using a traditional approach with selenomethionine M66A COMP as the native protein, because it demonstrated a higher stability of unit cell dimensions upon soaking (note the significant nonisomorphism between the native and M66A data). This search produced two useful derivatives. Alternatively, we attempted to make use of a putative axial hydrophobic cavity in the model pentameric coiled coil by preparing the xenon derivative. After subjecting native crystals to a xenon pressure between 2 and 5 bar, only weak binding was detected. However, with an improved system, we were able to apply pressure of 10 bar to the M66A mutant crystal in a standard 0.5-mm glass capillary, which resulted in a useful derivative.
  • 36
    • 10544240472 scopus 로고    scopus 로고
    • note
    • 72.
  • 37
    • 10544254372 scopus 로고    scopus 로고
    • note
    • Supported in part by Swiss National Science Foundation grant 31-32251.91 to J.E. We thank J. N. Jansonius for support and for providing access to x-ray equipment, and also for valuable comments on the manuscript. Coordinates have been deposited in the Brookhaven Protein Bank (entry code, 1VDF).


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