6xm1

SM Protein Vps45 in Complex with Qa SNARE Tlg2

spinqualitylabelsall models 6xm1, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6xm1 is a 4 chain structure with sequence from Chaetomium thermophilum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0S539_CHATD 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Vacuolar protein sorting-associated protein 3D structures

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