8WB6
Cryo-EM structure of Snf7 N-terminal domain in outer coils of spiral polymers
Summary for 8WB6
| Entry DOI | 10.2210/pdb8wb6/pdb |
| EMDB information | 37416 |
| Descriptor | SNF7 isoform 1 (1 entity in total) |
| Functional Keywords | membrane fission, spiral polymers, n-terminal domain, "open" status, protein transport |
| Biological source | Saccharomyces cerevisiae (brewer's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 27020.12 |
| Authors | Liu, M.D.,Shen, Q.T. (deposition date: 2023-09-08, release date: 2024-05-29, Last modification date: 2024-06-05) |
| Primary citation | Liu, M.,Liu, Y.,Song, T.,Yang, L.,Qi, L.,Zhang, Y.Z.,Wang, Y.,Shen, Q.T. Three-dimensional architecture of ESCRT-III flat spirals on the membrane. Proc.Natl.Acad.Sci.USA, 121:e2319115121-e2319115121, 2024 Cited by PubMed Abstract: The endosomal sorting complexes required for transport (ESCRTs) are responsible for membrane remodeling in many cellular processes, such as multivesicular body biogenesis, viral budding, and cytokinetic abscission. ESCRT-III, the most abundant ESCRT subunit, assembles into flat spirals as the primed state, essential to initiate membrane invagination. However, the three-dimensional architecture of ESCRT-III flat spirals remained vague for decades due to highly curved filaments with a small diameter and a single preferred orientation on the membrane. Here, we unveiled that yeast Snf7, a component of ESCRT-III, forms flat spirals on the lipid monolayers using cryogenic electron microscopy. We developed a geometry-constrained Euler angle-assigned reconstruction strategy and obtained moderate-resolution structures of Snf7 flat spirals with varying curvatures. Our analyses showed that Snf7 subunits recline on the membrane with N-terminal motifs α0 as anchors, adopt an open state with fused α2/3 helices, and bend α2/3 gradually from the outer to inner parts of flat spirals. In all, we provide the orientation and conformations of ESCRT-III flat spirals on the membrane and unveil the underlying assembly mechanism, which will serve as the initial step in understanding how ESCRTs drive membrane abscission. PubMed: 38709931DOI: 10.1073/pnas.2319115121 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7.1 Å) |
Structure validation
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