7udb: Difference between revisions
m Protected "7udb" [edit=sysop:move=sysop] |
No edit summary |
||
(2 intermediate revisions by the same user not shown) | |||
Line 1: | Line 1: | ||
==Cryo-EM structure of a synaptobrevin-Munc18-1-syntaxin-1 complex class 2== | |||
<StructureSection load='7udb' size='340' side='right'caption='[[7udb]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7udb]] is a 3 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=7UDB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UDB FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</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=7udb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7udb OCA], [https://pdbe.org/7udb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7udb RCSB], [https://www.ebi.ac.uk/pdbsum/7udb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7udb ProSAT]</span></td></tr> | |||
</table> | |||
== 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;"> | |||
== Publication Abstract from PubMed == | |||
Munc18-1 forms a template to organize assembly of the neuronal SNARE complex that triggers neurotransmitter release, binding first to a closed conformation of syntaxin-1 where its amino-terminal region interacts with the SNARE motif, and later binding to synaptobrevin. However, the mechanism of SNARE complex assembly remains unclear. Here, we report two cryo-EM structures of Munc18-1 bound to cross-linked syntaxin-1 and synaptobrevin. The structures allow visualization of how syntaxin-1 opens and reveal how part of the syntaxin-1 amino-terminal region can help nucleate interactions between the amino termini of the syntaxin-1 and synaptobrevin SNARE motifs, while their carboxyl termini bind to distal sites of Munc18-1. These observations, together with mutagenesis, SNARE complex assembly experiments, and fusion assays with reconstituted proteoliposomes, support a model whereby these interactions are critical to initiate SNARE complex assembly and multiple energy barriers enable diverse mechanisms for exquisite regulation of neurotransmitter release. | |||
SNARE assembly enlightened by cryo-EM structures of a synaptobrevin-Munc18-1-syntaxin-1 complex.,Stepien KP, Xu J, Zhang X, Bai XC, Rizo J Sci Adv. 2022 Jun 24;8(25):eabo5272. doi: 10.1126/sciadv.abo5272. Epub 2022 Jun , 22. PMID:35731863<ref>PMID:35731863</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7udb" style="background-color:#fffaf0;"></div> | ||
[[Category: Bai | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Syntaxin 3D structures|Syntaxin 3D structures]] | ||
[[Category: | *[[Syntaxin-binding protein|Syntaxin-binding protein]] | ||
*[[Vesicle-associated membrane protein 3D structures|Vesicle-associated membrane protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Rattus norvegicus]] | |||
[[Category: Bai X]] | |||
[[Category: Rizo J]] | |||
[[Category: Stepien KP]] | |||
[[Category: Xu J]] | |||
[[Category: Zhang X]] |
Latest revision as of 14:36, 23 October 2024
Cryo-EM structure of a synaptobrevin-Munc18-1-syntaxin-1 complex class 2Cryo-EM structure of a synaptobrevin-Munc18-1-syntaxin-1 complex class 2
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 PubMedMunc18-1 forms a template to organize assembly of the neuronal SNARE complex that triggers neurotransmitter release, binding first to a closed conformation of syntaxin-1 where its amino-terminal region interacts with the SNARE motif, and later binding to synaptobrevin. However, the mechanism of SNARE complex assembly remains unclear. Here, we report two cryo-EM structures of Munc18-1 bound to cross-linked syntaxin-1 and synaptobrevin. The structures allow visualization of how syntaxin-1 opens and reveal how part of the syntaxin-1 amino-terminal region can help nucleate interactions between the amino termini of the syntaxin-1 and synaptobrevin SNARE motifs, while their carboxyl termini bind to distal sites of Munc18-1. These observations, together with mutagenesis, SNARE complex assembly experiments, and fusion assays with reconstituted proteoliposomes, support a model whereby these interactions are critical to initiate SNARE complex assembly and multiple energy barriers enable diverse mechanisms for exquisite regulation of neurotransmitter release. SNARE assembly enlightened by cryo-EM structures of a synaptobrevin-Munc18-1-syntaxin-1 complex.,Stepien KP, Xu J, Zhang X, Bai XC, Rizo J Sci Adv. 2022 Jun 24;8(25):eabo5272. doi: 10.1126/sciadv.abo5272. Epub 2022 Jun , 22. PMID:35731863[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
|