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8PFH

Crystal structure of the yeast septin complex Shs1-Cdc12-Cdc3-Cdc10

Summary for 8PFH
Entry DOI10.2210/pdb8pfh/pdb
DescriptorCDC10 isoform 1, Cell division control protein 3, CDC12 isoform 1, ... (5 entities in total)
Functional Keywordsseptins, complex, structural protein
Biological sourceSaccharomyces cerevisiae (baker's yeast)
More
Total number of polymer chains4
Total formula weight148970.46
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 citationGrupp, 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: 38184752
DOI: 10.1038/s42003-023-05734-w
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.24 Å)
Structure validation

226707

数据于2024-10-30公开中

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