6ZW5
C15 symmetry: Bacterial Vipp1 and PspA are members of the ancient ESCRT-III membrane-remodeling superfamily.
This is a non-PDB format compatible entry.
Summary for 6ZW5
| Entry DOI | 10.2210/pdb6zw5/pdb |
| EMDB information | 11468 11469 11481 |
| Descriptor | vipp1 (1 entity in total) |
| Functional Keywords | membrane remodelling, lipid binding protein |
| Biological source | Nostoc punctiforme |
| Total number of polymer chains | 90 |
| Total formula weight | 2587091.49 |
| Authors | Liu, J.W.,Tassinari, M.,Souza, D.P.,Naskar, S.,Noel, J.K.,Bohuszewicz, O.,Buck, M.,Williams, T.A.,Baum, B.,Low, H.H. (deposition date: 2020-07-27, release date: 2021-08-04, Last modification date: 2024-07-10) |
| Primary citation | Liu, J.,Tassinari, M.,Souza, D.P.,Naskar, S.,Noel, J.K.,Bohuszewicz, O.,Buck, M.,Williams, T.A.,Baum, B.,Low, H.H. Bacterial Vipp1 and PspA are members of the ancient ESCRT-III membrane-remodeling superfamily. Cell, 184:3660-3673.e18, 2021 Cited by PubMed Abstract: Membrane remodeling and repair are essential for all cells. Proteins that perform these functions include Vipp1/IM30 in photosynthetic plastids, PspA in bacteria, and ESCRT-III in eukaryotes. Here, using a combination of evolutionary and structural analyses, we show that these protein families are homologous and share a common ancient evolutionary origin that likely predates the last universal common ancestor. This homology is evident in cryo-electron microscopy structures of Vipp1 rings from the cyanobacterium Nostoc punctiforme presented over a range of symmetries. Each ring is assembled from rungs that stack and progressively tilt to form dome-shaped curvature. Assembly is facilitated by hinges in the Vipp1 monomer, similar to those in ESCRT-III proteins, which allow the formation of flexible polymers. Rings have an inner lumen that is able to bind and deform membranes. Collectively, these data suggest conserved mechanistic principles that underlie Vipp1, PspA, and ESCRT-III-dependent membrane remodeling across all domains of life. PubMed: 34166615DOI: 10.1016/j.cell.2021.05.041 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7 Å) |
Structure validation
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