4jeh: Difference between revisions
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==Crystal Structure of Munc18a and Syntaxin1 lacking N-peptide complex== | ==Crystal Structure of Munc18a and Syntaxin1 lacking N-peptide complex== | ||
<StructureSection load='4jeh' size='340' side='right' caption='[[4jeh]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='4jeh' size='340' side='right'caption='[[4jeh]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jeh]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4jeh]] 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=4JEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JEH FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=4jeh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jeh OCA], [https://pdbe.org/4jeh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jeh RCSB], [https://www.ebi.ac.uk/pdbsum/4jeh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jeh ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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 == | ||
| Line 19: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 4jeh" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4jeh" 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: | [[Category: Large Structures]] | ||
[[Category: Burkhardt | [[Category: Rattus norvegicus]] | ||
[[Category: Colbert | [[Category: Burkhardt P]] | ||
[[Category: Fasshauer | [[Category: Colbert KN]] | ||
[[Category: Hattendorf | [[Category: Fasshauer D]] | ||
[[Category: Weis | [[Category: Hattendorf DA]] | ||
[[Category: Weiss | [[Category: Weis WI]] | ||
[[Category: Weiss TM]] | |||
Latest revision as of 18:41, 20 September 2023
Crystal Structure of Munc18a and Syntaxin1 lacking N-peptide complexCrystal Structure of Munc18a and Syntaxin1 lacking N-peptide complex
Structural highlights
FunctionSTXB1_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 PubMedIn 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 AlsoReferences
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