메뉴 건너뛰기




Volumn 1, Issue 3, 1999, Pages 175-182

Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CARRIER PROTEIN; MEMBRANE PROTEIN; N ETHYLMALEIMIDE; N ETHYLMALEIMIDE SENSITIVE FACTOR; PEPTIDE FRAGMENT; RECOMBINANT PROTEIN; SNARE PROTEIN; VESICULAR TRANSPORT PROTEIN;

EID: 0033163807     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/11097     Document Type: Article
Times cited : (84)

References (50)
  • 1
    • 0030992881 scopus 로고    scopus 로고
    • The roles of NSF, SNAPs and SNAREs during membrane fusion
    • Woodman, P. G. The roles of NSF, SNAPs and SNAREs during membrane fusion. Biochim. Biophys. Acta 1357, 155-172 (1997).
    • (1997) Biochim. Biophys. Acta , vol.1357 , pp. 155-172
    • Woodman, P.G.1
  • 2
    • 0032054866 scopus 로고    scopus 로고
    • Analysis of regulated exocytosis in adrenal chromaffin cells: Insights into NSF/SNAP/SNARE function
    • Burgoyne, R. D. & Morgan, A. Analysis of regulated exocytosis in adrenal chromaffin cells: insights into NSF/SNAP/SNARE function. Bioessays 20, 328-335 (1998).
    • (1998) Bioessays , vol.20 , pp. 328-335
    • Burgoyne, R.D.1    Morgan, A.2
  • 4
    • 0027413655 scopus 로고
    • SNAP receptors implicated in vesicle targeting and fusion
    • Söllner, T. et al. SNAP receptors implicated in vesicle targeting and fusion. Nature 362, 318-324 (1993).
    • (1993) Nature , vol.362 , pp. 318-324
    • Söllner, T.1
  • 6
    • 0029980441 scopus 로고    scopus 로고
    • Sec18p (NSF)-driven release of Sec17p (α-SNAP) can precede docking and fusion of yeast vacuoles
    • Mayer, A., Wickner, W. & Haas, A. Sec18p (NSF)-driven release of Sec17p (α-SNAP) can precede docking and fusion of yeast vacuoles. Cell 85, 83-94 (1996).
    • (1996) Cell , vol.85 , pp. 83-94
    • Mayer, A.1    Wickner, W.2    Haas, A.3
  • 8
    • 0031040763 scopus 로고    scopus 로고
    • Docking of yeast vacuoles is catalyzed by the ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF)
    • Mayer, A. & Wickner, W. Docking of yeast vacuoles is catalyzed by the ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF). J. Cell Biol. 136, 307-317 (1997).
    • (1997) J. Cell Biol. , vol.136 , pp. 307-317
    • Mayer, A.1    Wickner, W.2
  • 9
    • 0031942615 scopus 로고    scopus 로고
    • A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion
    • Ungermann, C., Nichols, B. J., Pelham, H. R. B. & Wickner, W. A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion. J. Cell Biol. 140, 61-69 (1998).
    • (1998) J. Cell Biol. , vol.140 , pp. 61-69
    • Ungermann, C.1    Nichols, B.J.2    Pelham, H.R.B.3    Wickner, W.4
  • 10
    • 0032506543 scopus 로고    scopus 로고
    • Defining the functions of trans-SNARE pairs
    • Ungermann, C., Sato, K. & Wickner, W. Defining the functions of trans-SNARE pairs. Nature 396, 543-548 (1998).
    • (1998) Nature , vol.396 , pp. 543-548
    • Ungermann, C.1    Sato, K.2    Wickner, W.3
  • 11
    • 0032127472 scopus 로고    scopus 로고
    • NSF binding to GluR2 regulates synaptic transmission
    • Nishimune, A. et al. NSF binding to GluR2 regulates synaptic transmission. Neuron 21, 87-97 (1998).
    • (1998) Neuron , vol.21 , pp. 87-97
    • Nishimune, A.1
  • 12
    • 0032125884 scopus 로고    scopus 로고
    • The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-dependent interaction with NSF and alpha- and beta-SNAPs
    • Osten, P. et al. The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-dependent interaction with NSF and alpha- and beta-SNAPs. Neuron 21, 99-110 (1998).
    • (1998) Neuron , vol.21 , pp. 99-110
    • Osten, P.1
  • 13
    • 0032143945 scopus 로고    scopus 로고
    • Interaction of the N-ethylmaleimide-sensitive factor with AMPA receptors
    • Song, I. et al. Interaction of the N-ethylmaleimide-sensitive factor with AMPA receptors. Neuron 21, 393-400 (1998).
    • (1998) Neuron , vol.21 , pp. 393-400
    • Song, I.1
  • 14
    • 0033574530 scopus 로고    scopus 로고
    • Identification of NSF as a β-arrestin1-binding protein
    • McDonald, P. H. et al. Identification of NSF as a β-arrestin1-binding protein. J. Biol. Chem. 274, 10677-10680 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 10677-10680
    • McDonald, P.H.1
  • 15
    • 0024342254 scopus 로고
    • A fusion protein required for vesicle-mediated transport in both mammalian cells and yeast
    • Wilson, D. W. et al. A fusion protein required for vesicle-mediated transport in both mammalian cells and yeast. Nature 339, 355-359 (1989).
    • (1989) Nature , vol.339 , pp. 355-359
    • Wilson, D.W.1
  • 16
    • 0027474007 scopus 로고
    • Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport
    • Tagaya, M., Wilson, D. W., Brunner, M., Arango, N. & Rothman, J. E. Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport. J. Biol. Chem. 268, 2662-2666 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 2662-2666
    • Tagaya, M.1    Wilson, D.W.2    Brunner, M.3    Arango, N.4    Rothman, J.E.5
  • 17
    • 0032969563 scopus 로고    scopus 로고
    • +: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • +: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27-43 (1999).
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.I.3    Koonin, E.V.4
  • 18
    • 0029089959 scopus 로고
    • An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments
    • Rabouille, C., Levine, T. P., Peters, J.-M. & Warren, G. An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments. Cell 82, 905-914 (1995).
    • (1995) Cell , vol.82 , pp. 905-914
    • Rabouille, C.1    Levine, T.P.2    Peters, J.-M.3    Warren, G.4
  • 19
    • 0028132782 scopus 로고
    • N-ethylmaleimide-sensitive fusion protein: A trimeric ATPase whose hydrolysis of ATP is required for membrane fusion
    • Whiteheart, S. W. et al. N-ethylmaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion. J. Cell. Biol. 126, 945-954 (1994).
    • (1994) J. Cell. Biol. , vol.126 , pp. 945-954
    • Whiteheart, S.W.1
  • 20
    • 0028802295 scopus 로고
    • Each domain of the N-ethylmaleimide-sensitive fusion protein contributes to its transport activity
    • Nagiec, E. E., Bernstein, A. & Whiteheart, S. W. Each domain of the N-ethylmaleimide-sensitive fusion protein contributes to its transport activity. J. Biol. Chem. 270, 29182-29188 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 29182-29188
    • Nagiec, E.E.1    Bernstein, A.2    Whiteheart, S.W.3
  • 21
    • 0031576237 scopus 로고    scopus 로고
    • N-ethylmaleimide-sensitive fusion protein contains high and low affinity ATP-binding sites that are functionally distinct
    • Matveeva, E. A., He, P. & Whiteheart, S. W. N-ethylmaleimide-sensitive fusion protein contains high and low affinity ATP-binding sites that are functionally distinct. J. Biol. Chem. 272, 26413-26418 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 26413-26418
    • Matveeva, E.A.1    He, P.2    Whiteheart, S.W.3
  • 22
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein
    • Lenzen, C. U., Steinmann, D., Whiteheart, S. W. & Weis, W. I. Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein. Cell 94, 525-536 (1998).
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 23
    • 0031715606 scopus 로고    scopus 로고
    • Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP
    • Yu, R. C., Hanson, P. I., Jahn, R. & Brünger, A. T. Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP. Nature Struct. Biol. 5, 803-811 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 803-811
    • Yu, R.C.1    Hanson, P.I.2    Jahn, R.3    Brünger, A.T.4
  • 24
    • 0028149757 scopus 로고
    • The ATPase activity of N-ethylmaleimide-sensitive fusion protein (NSF) is regulated by soluble NSF attachment proteins
    • Morgan, A., Dimaline, R. & Burgoyne, R. D. The ATPase activity of N-ethylmaleimide-sensitive fusion protein (NSF) is regulated by soluble NSF attachment proteins. J. Biol. Chem. 269, 29347-29350 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 29347-29350
    • Morgan, A.1    Dimaline, R.2    Burgoyne, R.D.3
  • 25
    • 0030682481 scopus 로고    scopus 로고
    • Stimulation of NSF ATPase activity by α-SNAP is required for SNARE complex disassembly and exocytosis
    • Barnard, R. J. O., Morgan, A. & Burgoyne, R. D. Stimulation of NSF ATPase activity by α-SNAP is required for SNARE complex disassembly and exocytosis. J. Cell Biol. 139, 875-883 (1997).
    • (1997) J. Cell Biol. , vol.139 , pp. 875-883
    • Barnard, R.J.O.1    Morgan, A.2    Burgoyne, R.D.3
  • 26
    • 0032544437 scopus 로고    scopus 로고
    • The effects of SNAP/SNARE complexes on the ATPase of NSF
    • Matveeva, E. & Whiteheart, S. W. The effects of SNAP/SNARE complexes on the ATPase of NSF. FEBS Lett. 435, 211-214 (1998).
    • (1998) FEBS Lett. , vol.435 , pp. 211-214
    • Matveeva, E.1    Whiteheart, S.W.2
  • 27
    • 0024094923 scopus 로고
    • Characterization of a component of the yeast secretion machinery: Identification of the SEC18 gene product
    • Eakle, K. A., Bernstein, M. & Emr, S. D. Characterization of a component of the yeast secretion machinery: identification of the SEC18 gene product. Mol. Cell. Biol. 8, 4098-4109 (1988).
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4098-4109
    • Eakle, K.A.1    Bernstein, M.2    Emr, S.D.3
  • 28
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson, P. I., Roth, R., Morisaki, H., Jahn, R. & Heuser, J. E. Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90, 523-535 (1997).
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 29
    • 0033080967 scopus 로고    scopus 로고
    • A six-stranded double-psi β barrel is shared by several protein superfamilies
    • Castillo, R. M. et al. A six-stranded double-psi β barrel is shared by several protein superfamilies. Structure 7, 227-236 (1999).
    • (1999) Structure , vol.7 , pp. 227-236
    • Castillo, R.M.1
  • 30
    • 0029163609 scopus 로고
    • Distinct roles for N-ethylmaleimide-sensitive fusion protein (NSF) suggested by the identification of a second Drosophila NSF homolog
    • Pallanck, L. et al. Distinct roles for N-ethylmaleimide-sensitive fusion protein (NSF) suggested by the identification of a second Drosophila NSF homolog. J. Biol. Chem. 270, 18742-18744 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 18742-18744
    • Pallanck, L.1
  • 31
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. & Sander, C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138 (1993).
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 32
    • 0027179878 scopus 로고
    • Crystal structure of active elongation factor Tu reveals major domain rearrangements
    • Berchtold, H. et al. Crystal structure of active elongation factor Tu reveals major domain rearrangements. Nature 365, 126-132 (1993).
    • (1993) Nature , vol.365 , pp. 126-132
    • Berchtold, H.1
  • 33
    • 0027917990 scopus 로고
    • The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation
    • Kjeldgaard, M., Nissen, P., Thirup, S. & Nyborg, J. The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure 1, 35-50 (1993).
    • (1993) Structure , vol.1 , pp. 35-50
    • Kjeldgaard, M.1    Nissen, P.2    Thirup, S.3    Nyborg, J.4
  • 34
    • 0031793928 scopus 로고    scopus 로고
    • Iterated profile searches with PSI-BLAST - A tool for discovery in protein databases
    • Altschul, S. F. & Koonin, E. V. Iterated profile searches with PSI-BLAST - a tool for discovery in protein databases. Trends Biochem. Sci. 23, 444-447 (1998).
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 444-447
    • Altschul, S.F.1    Koonin, E.V.2
  • 35
    • 0028835784 scopus 로고
    • SNAPs and NSF: General members of the fusion apparatus
    • Whiteheart, S. W. & Kubalek, E. W. SNAPs and NSF: general members of the fusion apparatus. Trends Cell Biol. 5, 64-68 (1995).
    • (1995) Trends Cell Biol. , vol.5 , pp. 64-68
    • Whiteheart, S.W.1    Kubalek, E.W.2
  • 36
    • 0029004741 scopus 로고
    • Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro
    • Hayishi, T., Yamasaki, S., Nauenburg, S., Binz, T. & Niemann, H. Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro. EMBO J. 14, 2317-2325 (1995).
    • (1995) EMBO J. , vol.14 , pp. 2317-2325
    • Hayishi, T.1    Yamasaki, S.2    Nauenburg, S.3    Binz, T.4    Niemann, H.5
  • 37
    • 0030790695 scopus 로고    scopus 로고
    • p47 is a cofactor for p97-mediated membrane fusion
    • Kondo, H. et al. p47 is a cofactor for p97-mediated membrane fusion. Nature 388, 75-78 (1997).
    • (1997) Nature , vol.388 , pp. 75-78
    • Kondo, H.1
  • 38
    • 0032214690 scopus 로고    scopus 로고
    • Arrangement of subunits in 20 S particles consisting of NSF, SNAPs, and SNARE complexes
    • Hohl, T. M. et al. Arrangement of subunits in 20 S particles consisting of NSF, SNAPs, and SNARE complexes. Mol. Cell 2, 539-548 (1998).
    • (1998) Mol. Cell , vol.2 , pp. 539-548
    • Hohl, T.M.1
  • 39
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase - A splendid molecular machine
    • Boyer, P. D. The ATP synthase - a splendid molecular machine. Annu. Rev. Biochem. 66, 717-749 (1997).
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 40
    • 0032568695 scopus 로고    scopus 로고
    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120° steps
    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120° steps. Cell 93, 1117-1124 (1998).
    • (1998) Cell , vol.93 , pp. 1117-1124
    • Yasuda, R.1    Noji, H.2    Kinosita, K.3    Yoshida, M.4
  • 41
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson, W. A., Horton, J. R. & LeMaster, D. M. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J. 9, 1665-1672 (1990).
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3
  • 42
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system (CNS): A new software system for macromolecular structure determination
    • Brünger, A. T. et al. Crystallography and NMR system (CNS): a new software system for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 43
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 44
    • 0000019861 scopus 로고
    • The use of anomalous scattering effects to phase diffraction patterns from macromolecules
    • Phillips, J. C. & Hodgson, K. O. The use of anomalous scattering effects to phase diffraction patterns from macromolecules. Acta Crystallogr. A 36, 856-864 (1980).
    • (1980) Acta Crystallogr. A , vol.36 , pp. 856-864
    • Phillips, J.C.1    Hodgson, K.O.2
  • 45
    • 0030038545 scopus 로고    scopus 로고
    • Direct observation of protein solvation and discrete disorder with experimental crystallographic phases
    • Burling, F. T., Weis, W. I., Flaherty, K. M. & Brünger, A. T. Direct observation of protein solvation and discrete disorder with experimental crystallographic phases. Science 271, 72-77 (1996).
    • (1996) Science , vol.271 , pp. 72-77
    • Burling, F.T.1    Weis, W.I.2    Flaherty, K.M.3    Brünger, A.T.4
  • 46
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J.-Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for the building of protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 47
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475 (1992).
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 48
    • 0000649842 scopus 로고    scopus 로고
    • Improved structure refinement through maximum likelihood
    • Pannu, N. S. & Read, R. J. Improved structure refinement through maximum likelihood. Acta Crystallogr. A 52, 659-668 (1996).
    • (1996) Acta Crystallogr. A , vol.52 , pp. 659-668
    • Pannu, N.S.1    Read, R.J.2
  • 49
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf, R. M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. 15, 133-138 (1997).
    • (1997) J. Mol. Graph. , vol.15 , pp. 133-138
    • Esnouf, R.M.1
  • 50
    • 5844370843 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of N-ethylmaleimide sensitive factor reveals possible α-SNAP binding site and unexpected structural similarity to EfTu
    • Yu, R. C., Jahn, R. & Brünger, A. T. Crystal structure of the N-terminal domain of N-ethylmaleimide sensitive factor reveals possible α-SNAP binding site and unexpected structural similarity to EfTu. Mol. Cell (in the press).
    • Mol. Cell (in the Press)
    • Yu, R.C.1    Jahn, R.2    Brünger, A.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.