9GD4
Crystal structure of septin complex Shs1-Cdc12-Cdc3-Cdc10 from Saccharomyces cerevisiae
Summary for 9GD4
| Entry DOI | 10.2210/pdb9gd4/pdb |
| Descriptor | Cell division control protein 10, Cell division control protein 3, Cell division control protein 12, ... (8 entities in total) |
| Functional Keywords | septins, complex, guanine nucleotide binding protein, structural protein |
| Biological source | Saccharomyces cerevisiae (brewer's yeast) More |
| Total number of polymer chains | 4 |
| Total formula weight | 149090.82 |
| Authors | Grupp, B.,Seifermann, J.,Gerhardt, S.,Gronemeyer, T. (deposition date: 2024-08-04, release date: 2025-02-05, Last modification date: 2025-08-20) |
| Primary citation | Grupp, B.,Graser, J.B.,Seifermann, J.,Gerhardt, S.,Lemkul, J.A.,Gehrke, J.F.,Johnsson, N.,Gronemeyer, T. Interface integrity in septin protofilaments is maintained by an arginine residue conserved from yeast to man. Mol.Biol.Cell, 36:ar59-ar59, 2025 Cited by PubMed Abstract: The septins are conserved, filament-forming, guanine nucleotide binding cytoskeletal proteins. They assemble into palindromic protofilaments which polymerize further into higher-ordered structures that participate in essential intracellular processes such as cytokinesis or polarity establishment. Septins belong structurally to the P-Loop NTPases but, unlike their relatives Ras or Rho, do not mediate signals to effectors through GTP binding and hydrolysis. Biochemical approaches addressing how and why septins utilize nucleotides are hampered by the lack of nucleotide-free complexes. Using molecular dynamics simulations, we determined structural alterations and intersubunit binding free energies in human and yeast septin dimer structures and in their generated apo forms. An interchain salt bridge network around the septin unique β-meander, conserved across all kingdoms of septin containing species, is destabilized upon nucleotide removal, concomitant with disruption of the entire G-interface. Within this network, we confirmed a conserved arginine residue, which coordinates the guanine base of the nucleotide, as the central interaction hub. The essential role of this arginine for interface integrity was experimentally confirmed to be conserved in septins from yeast to human. PubMed: 40137961DOI: 10.1091/mbc.E25-01-0041 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.039 Å) |
Structure validation
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