6xmd: Difference between revisions
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==SM Protein Vps45 in Complex with Qa SNARE Tlg2 (1-310)== | |||
<StructureSection load='6xmd' size='340' side='right'caption='[[6xmd]], [[Resolution|resolution]] 3.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6xmd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XMD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XMD FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.9Å</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=6xmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xmd OCA], [https://pdbe.org/6xmd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xmd RCSB], [https://www.ebi.ac.uk/pdbsum/6xmd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xmd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/G0S539_CHATD G0S539_CHATD] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Fusion of intracellular trafficking vesicles is mediated by the assembly of SNARE proteins into membrane-bridging complexes. SNARE-mediated membrane fusion requires Sec1/Munc18-family (SM) proteins, SNARE chaperones that can function as templates to catalyze SNARE complex assembly. Paradoxically, the SM protein Munc18-1 traps the Qa-SNARE protein syntaxin-1 in an autoinhibited closed conformation. Here we present the structure of a second SM-Qa-SNARE complex, Vps45-Tlg2. Strikingly, Vps45 holds Tlg2 in an open conformation, with its SNARE motif disengaged from its Habc domain and its linker region unfolded. The domain 3a helical hairpin of Vps45 is unfurled, exposing the presumptive R-SNARE binding site to allow template complex formation. Although Tlg2 has a pronounced tendency to form homo-tetramers, Vps45 can rescue Tlg2 tetramers into stoichiometric Vps45-Tlg2 complexes. Our findings demonstrate that SM proteins can engage Qa-SNAREs using at least two different modes, one in which the SNARE is closed and one in which it is open. | |||
The Sec1/Munc18 protein Vps45 holds the Qa-SNARE Tlg2 in an open conformation.,Eisemann TJ, Allen F, Lau K, Shimamura GR, Jeffrey PD, Hughson FM Elife. 2020 Aug 17;9. pii: 60724. doi: 10.7554/eLife.60724. PMID:32804076<ref>PMID:32804076</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6xmd" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chaetomium thermophilum]] | |||
[[Category: Large Structures]] | |||
[[Category: Eisemann TJ]] | |||
[[Category: Hughson FM]] | |||
[[Category: Jeffrey PD]] | |||
Latest revision as of 17:55, 18 October 2023
SM Protein Vps45 in Complex with Qa SNARE Tlg2 (1-310)SM Protein Vps45 in Complex with Qa SNARE Tlg2 (1-310)
Structural highlights
FunctionPublication Abstract from PubMedFusion of intracellular trafficking vesicles is mediated by the assembly of SNARE proteins into membrane-bridging complexes. SNARE-mediated membrane fusion requires Sec1/Munc18-family (SM) proteins, SNARE chaperones that can function as templates to catalyze SNARE complex assembly. Paradoxically, the SM protein Munc18-1 traps the Qa-SNARE protein syntaxin-1 in an autoinhibited closed conformation. Here we present the structure of a second SM-Qa-SNARE complex, Vps45-Tlg2. Strikingly, Vps45 holds Tlg2 in an open conformation, with its SNARE motif disengaged from its Habc domain and its linker region unfolded. The domain 3a helical hairpin of Vps45 is unfurled, exposing the presumptive R-SNARE binding site to allow template complex formation. Although Tlg2 has a pronounced tendency to form homo-tetramers, Vps45 can rescue Tlg2 tetramers into stoichiometric Vps45-Tlg2 complexes. Our findings demonstrate that SM proteins can engage Qa-SNAREs using at least two different modes, one in which the SNARE is closed and one in which it is open. The Sec1/Munc18 protein Vps45 holds the Qa-SNARE Tlg2 in an open conformation.,Eisemann TJ, Allen F, Lau K, Shimamura GR, Jeffrey PD, Hughson FM Elife. 2020 Aug 17;9. pii: 60724. doi: 10.7554/eLife.60724. PMID:32804076[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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