8PFH
Crystal structure of the yeast septin complex Shs1-Cdc12-Cdc3-Cdc10
Summary for 8PFH
Entry DOI | 10.2210/pdb8pfh/pdb |
Descriptor | CDC10 isoform 1, Cell division control protein 3, CDC12 isoform 1, ... (5 entities in total) |
Functional Keywords | septins, complex, structural protein |
Biological source | Saccharomyces cerevisiae (baker's yeast) More |
Total number of polymer chains | 4 |
Total formula weight | 148970.46 |
Authors | Grupp, B.,Denkhaus, L.,Gerhardt, S.,Gronemeyer, T. (deposition date: 2023-06-16, release date: 2023-12-06, Last modification date: 2024-02-21) |
Primary citation | Grupp, B.,Denkhaus, L.,Gerhardt, S.,Vogele, M.,Johnsson, N.,Gronemeyer, T. The structure of a tetrameric septin complex reveals a hydrophobic element essential for NC-interface integrity. Commun Biol, 7:48-48, 2024 Cited by PubMed Abstract: The septins of the yeast Saccharomyces cerevisiae assemble into hetero-octameric rods by alternating interactions between neighboring G-domains or N- and C-termini, respectively. These rods polymerize end to end into apolar filaments, forming a ring beneath the prospective new bud that expands during the cell cycle into an hourglass structure. The hourglass finally splits during cytokinesis into a double ring. Understanding these transitions as well as the plasticity of the higher order assemblies requires a detailed knowledge of the underlying structures. Here we present the first X-ray crystal structure of a tetrameric Shs1-Cdc12-Cdc3-Cdc10 complex at a resolution of 3.2 Å. Close inspection of the NC-interfaces of this and other septin structures reveals a conserved contact motif that is essential for NC-interface integrity of yeast and human septins in vivo and in vitro. Using the tetrameric structure in combination with AlphaFold-Multimer allowed us to propose a model of the octameric septin rod. PubMed: 38184752DOI: 10.1038/s42003-023-05734-w PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.24 Å) |
Structure validation
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