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| | ==Crystal Structure of Munc18a and Syntaxin1 with native N-terminus complex== | | ==Crystal Structure of Munc18a and Syntaxin1 with native N-terminus complex== |
| - | <StructureSection load='4jeu' size='340' side='right' caption='[[4jeu]], [[Resolution|resolution]] 3.20Å' scene=''> | + | <StructureSection load='4jeu' size='340' side='right'caption='[[4jeu]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4jeu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JEU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JEU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4jeu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JEU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JEU FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jeh|4jeh]]</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jeu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jeu OCA], [https://pdbe.org/4jeu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jeu RCSB], [https://www.ebi.ac.uk/pdbsum/4jeu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jeu ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Stxbp1, Unc18a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), Stx1a, Sap ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4jeu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jeu OCA], [http://pdbe.org/4jeu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jeu RCSB], [http://www.ebi.ac.uk/pdbsum/4jeu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jeu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/STXB1_RAT STXB1_RAT]] May participate in the regulation of synaptic vesicle docking and fusion, possibly through interaction with GTP-binding proteins. Essential for neurotransmission and binds syntaxin, a component of the synaptic vesicle fusion machinery probably in a 1:1 ratio. Can interact with syntaxins 1, 2, and 3 but not syntaxin 4. May play a role in determining the specificity of intracellular fusion reactions. [[http://www.uniprot.org/uniprot/STX1A_RAT STX1A_RAT]] Potentially involved in docking of synaptic vesicles at presynaptic active zones. May play a critical role in neurotransmitter exocytosis. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm. | + | [https://www.uniprot.org/uniprot/STXB1_RAT STXB1_RAT] May participate in the regulation of synaptic vesicle docking and fusion, possibly through interaction with GTP-binding proteins. Essential for neurotransmission and binds syntaxin, a component of the synaptic vesicle fusion machinery probably in a 1:1 ratio. Can interact with syntaxins 1, 2, and 3 but not syntaxin 4. May play a role in determining the specificity of intracellular fusion reactions. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4jeu" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4jeu" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Syntaxin 3D structures|Syntaxin 3D structures]] |
| | + | *[[Syntaxin-binding protein|Syntaxin-binding protein]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Large Structures]] |
| - | [[Category: Burkhardt, P]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Colbert, K N]] | + | [[Category: Burkhardt P]] |
| - | [[Category: Fasshauer, D]] | + | [[Category: Colbert KN]] |
| - | [[Category: Hattendorf, D A]] | + | [[Category: Fasshauer D]] |
| - | [[Category: Weis, W I]] | + | [[Category: Hattendorf DA]] |
| - | [[Category: Weiss, T M]] | + | [[Category: Weis WI]] |
| - | [[Category: Endocytosis-exocytosis complex]]
| + | [[Category: Weiss TM]] |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Neurotransmitter transport]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Protein complex]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Transport]]
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| Structural highlights
Function
STXB1_RAT May participate in the regulation of synaptic vesicle docking and fusion, possibly through interaction with GTP-binding proteins. Essential for neurotransmission and binds syntaxin, a component of the synaptic vesicle fusion machinery probably in a 1:1 ratio. Can interact with syntaxins 1, 2, and 3 but not syntaxin 4. May play a role in determining the specificity of intracellular fusion reactions.
Publication Abstract from PubMed
In neurons, soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) proteins drive the fusion of synaptic vesicles to the plasma membrane through the formation of a four-helix SNARE complex. Members of the Sec1/Munc18 protein family regulate membrane fusion through interactions with the syntaxin family of SNARE proteins. The neuronal protein Munc18a interacts with a closed conformation of the SNARE protein syntaxin1a (Syx1a) and with an assembled SNARE complex containing Syx1a in an open conformation. The N-peptide of Syx1a (amino acids 1-24) has been implicated in the transition of Munc18a-bound Syx1a to Munc18a-bound SNARE complex, but the underlying mechanism is not understood. Here we report the X-ray crystal structures of Munc18a bound to Syx1a with and without its native N-peptide (Syx1aDeltaN), along with small-angle X-ray scattering (SAXS) data for Munc18a bound to Syx1a, Syx1aDeltaN, and Syx1a L165A/E166A (LE), a mutation thought to render Syx1a in a constitutively open conformation. We show that all three complexes adopt the same global structure, in which Munc18a binds a closed conformation of Syx1a. We also identify a possible structural connection between the Syx1a N-peptide and SNARE domain that might be important for the transition of closed-to-open Syx1a in SNARE complex assembly. Although the role of the N-peptide in Munc18a-mediated SNARE complex assembly remains unclear, our results demonstrate that the N-peptide and LE mutation have no effect on the global conformation of the Munc18a-Syx1a complex.
Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation.,Colbert KN, Hattendorf DA, Weiss TM, Burkhardt P, Fasshauer D, Weis WI Proc Natl Acad Sci U S A. 2013 Jul 30;110(31):12637-42. doi:, 10.1073/pnas.1303753110. Epub 2013 Jul 15. PMID:23858467[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Colbert KN, Hattendorf DA, Weiss TM, Burkhardt P, Fasshauer D, Weis WI. Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation. Proc Natl Acad Sci U S A. 2013 Jul 30;110(31):12637-42. doi:, 10.1073/pnas.1303753110. Epub 2013 Jul 15. PMID:23858467 doi:http://dx.doi.org/10.1073/pnas.1303753110
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