| Author(s) | Sutton RB; Fasshauer D; Jahn R; Brunger AT
|
|---|
| Title | Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 angstrom resolution
|
|---|
| Source | NATURE 395(6700):347-353
|
|---|
| Date | 1998 SEP 24
|
|---|
| Type | Journal : Article
|
|---|
| LCR: 12 NCR: 50 LCS: 11 GCS: 629
| | Comment |
|
|---|
| Address | Yale Univ, Howard Hughes Med Inst, New Haven, CT 06520 USA
Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA
Max Planck Inst Biophys Chem, Dept Neurobiol, D-37077 Gottingen, Germany
|
|---|
| Abstract | The evolutionarily conserved SNARE proteins and their complexes are involved in the fusion of vesicles with their target membranes; however, the overall organization and structural details of these complexes are unknown. Here we report the X-ray crystal structure at 2.4 Angstrom resolution of a core synaptic fusion complex containing syntaxin-1A, synaptobrevin-II and SNAP-25B. The structure reveals a highly twisted and parallel four-helix bundle that differs from the bundles described for the haemagglutinin and HIV/SIV gp41 membrane-fusion proteins. Conserved leucine-zipper-like layers are found at the centre of the synaptic fusion complex. Embedded within these leucine-ripper layers is an ionic layer consisting of an arginine and three glutamine residues contributed from each of the four alpha-helices. These residues are highly conserved across the entire SNARE family. The regions flanking the leucine-zipper-like layers contain a hydrophobic core similar to that of more general four-helix-bundle proteins. The surface of the synaptic fusion complex is highly grooved and possesses distinct hydrophilic, hydrophobic and charged regions. These characteristics may be important for membrane fusion and for the binding of regulatory factors affecting neurotransmission.
|
|---|
| CR |
BERNARD A, 1995, CURR PROTOCOL PROTEI, P1
BLOCK MR, 1988, P NATL ACAD SCI USA, V85, P7852
BRICOGNE G, 1997, METHOD ENZYMOL, V276, P361
BRUNGER AT, 1998, ACTA CRYSTALLOGR D 5, V54, P905
BRUNGER AT, 1992, NATURE, V355, P472
BURLING FT, 1996, SCIENCE, V271, P72
CAFFREY M, 1998, EMBO J, V17, P4572
CHAN DC, 1998, CELL, V93, P681
CHAN DC, 1997, CELL, V89, P263
CRICK FHC, 1953, ACTA CRYSTALLOGR, V6, P689
ESNOUF RM, 1997, J MOL GRAPH MODEL, V15, P132
FASSHAUER D, 1998, BIOCHEMISTRY-US, V37, P10345
FASSHAUER D, 1997, J BIOL CHEM, V272, P4582
FASSHAUER D, 1997, J BIOL CHEM, V272, P28036
HANSON PI, 1997, CELL, V90, P523
HANSON PI, 1997, CURR OPIN NEUROBIOL, V7, P310
HANSON PI, 1995, J BIOL CHEM, V270, P16955
HAO JC, 1997, J NEUROSCI, V17, P1596
HARBURY PB, 1993, SCIENCE, V262, P1401
HAYASHI T, 1995, EMBO J, V14, P2317
HAYASHI T, 1994, EMBO J, V13, P5051
HENDRICKSON WA, 1985, METHOD ENZYMOL, V115, P252
HENDRICKSON WA, 1991, SCIENCE, V254, P51
JAHN R, 1994, ANN NY ACAD SCI, V733, P245
JONES TA, 1991, ACTA CRYSTALLOGR A, V47, P110
JORGENSEN WL, 1988, J AM CHEM SOC, V110, P1657
KEE Y, 1995, NEURON, V14, P991
LEAHY DJ, 1994, PROTEINS, V19, P48
LUPAS A, 1991, SCIENCE, V252, P1162
MALASHKEVICH VN, 1998, P NATL ACAD SCI USA, V95, P9134
NICHOLLS A, 1991, PROTEINS, V11, P281
NICHOLS BJ, 1997, NATURE, V387, P199
OTTO H, 1997, P NATL ACAD SCI USA, V94, P6197
OTWINOWSKI Z, 1997, METHOD ENZYMOL, V276, P307
OYLER GA, 1989, J CELL BIOL, V109, P3039
PANNU NS, IN PRESS ACTA CRYS D,
PHILLIPS JC, 1980, ACTA CRYSTALLOGR A, V36, P856
READ RJ, 1986, ACTA CRYSTALLOGR A, V42, P140
READ RJ, 1997, METHOD ENZYMOL, V277, P110
RICE LM, 1997, FEBS LETT, V415, P49
RICE LM, 1994, PROTEINS, V19, P277
SAIFEE O, 1998, MOL BIOL CELL, V9, P1235
SOLLNER T, 1993, CELL, V75, P409
SUDHOF TC, 1995, NATURE, V375, P645
WANG BC, 1985, METHOD ENZYMOL, V115, P90
WEIMBS T, 1998, TRENDS CELL BIOL, V8, P260
WEISSENHORN W, 1997, NATURE, V387, P426
WILSON IA, 1981, NATURE, V289, P366
WIMLEY WC, 1996, NAT STRUCT BIOL, V3, P842
ZHANG KYJ, 1990, ACTA CRYSTALLOGR A, V46, P41
|
|---|
|
|