6XJL

Structure of the SM protein Vps45

Summary for 6XJL

• Entry DOI: 10.2210/pdb6xjl/pdb
• Related: 6XM1 6XMD
• Descriptor: Vps45 (2 entities in total)
• Functional Keywords: membrane trafficking, sm protein, thermophile, transport protein
• Biological source: Chaetomium thermophilum
• Total number of polymer chains: 1
• Total formula weight: 71625.32

Authors

Jeffrey, P.D.,Shimamura, G.S.,Allen, F.,Hughson, F.M. (deposition date: 2020-06-24, release date: 2020-08-19, Last modification date: 2024-03-06)

Primary citation

Eisemann, T.J.,Allen, F.,Lau, K.,Shimamura, G.R.,Jeffrey, P.D.,Hughson, F.M.
The Sec1/Munc18 protein Vps45 holds the Qa-SNARE Tlg2 in an open conformation.
Elife, 9:-, 2020

PubMed Abstract: 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.

PubMed: 32804076
DOI: 10.7554/eLife.60724

Experimental method

X-RAY DIFFRACTION (2 Å)