1sfc

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(New page: 200px<br /><applet load="1sfc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sfc, resolution 2.40&Aring;" /> '''NEURONAL SYNAPTIC FU...)
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[[Image:1sfc.gif|left|200px]]<br /><applet load="1sfc" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1sfc, resolution 2.40&Aring;" />
caption="1sfc, resolution 2.40&Aring;" />
'''NEURONAL SYNAPTIC FUSION COMPLEX'''<br />
'''NEURONAL SYNAPTIC FUSION COMPLEX'''<br />
==Overview==
==Overview==
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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 A resolution of, a core synaptic fusion complex containing syntaxin-1 A, 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-zipper 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.
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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 A resolution of a core synaptic fusion complex containing syntaxin-1 A, 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-zipper 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.
==About this Structure==
==About this Structure==
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1SFC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with SR and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SFC OCA].
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1SFC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=SR:'>SR</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SFC OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Brunger, A.T.]]
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[[Category: Brunger, A T.]]
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[[Category: Sutton, R.B.]]
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[[Category: Sutton, R B.]]
[[Category: MPD]]
[[Category: MPD]]
[[Category: SR]]
[[Category: SR]]
[[Category: membrane fusion protein complex]]
[[Category: membrane fusion protein complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:20:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:00:52 2008''

Revision as of 13:00, 21 February 2008


1sfc, resolution 2.40Å

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NEURONAL SYNAPTIC FUSION COMPLEX

Overview

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 A resolution of a core synaptic fusion complex containing syntaxin-1 A, 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-zipper 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.

About this Structure

1SFC is a Protein complex structure of sequences from Rattus norvegicus with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution., Sutton RB, Fasshauer D, Jahn R, Brunger AT, Nature. 1998 Sep 24;395(6700):347-53. PMID:9759724

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