6DEI
Structure of Dse3-Csm1 complex
Summary for 6DEI
| Entry DOI | 10.2210/pdb6dei/pdb |
| Descriptor | Monopolin complex subunit CSM1, Protein DSE3, TRIETHYLENE GLYCOL, ... (5 entities in total) |
| Functional Keywords | monopolin, daughter cell-specific protein, protein binding-cell cycle complex, protein binding/cell cycle |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 4 |
| Total formula weight | 31752.56 |
| Authors | Singh, N.,Corbett, K.D. (deposition date: 2018-05-12, release date: 2018-10-03, Last modification date: 2023-10-11) |
| Primary citation | Singh, N.,Corbett, K.D. The budding-yeast RWD protein Csm1 scaffolds diverse protein complexes through a conserved structural mechanism. Protein Sci., 27:2094-2100, 2018 Cited by PubMed Abstract: RWD domains mediate protein-protein interactions in a variety of pathways in eukaryotes. In budding yeast, the RWD domain protein Csm1 is particularly versatile, assembling key complexes in the nucleolus and at meiotic kinetochores through multiple protein interaction surfaces. Here, we reveal a third functional context for Csm1 by identifying a new Csm1-interacting protein, Dse3. We show that Dse3 interacts with Csm1 in a structurally equivalent manner to its known binding partners Mam1 and Ulp2, despite these three proteins' lack of overall sequence homology. We theorize that the unique "clamp" structure of Csm1 and the loose sequence requirements for Csm1 binding have led to its incorporation into at least three different structural/signaling pathways in budding yeast. PubMed: 30252178DOI: 10.1002/pro.3515 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.699 Å) |
Structure validation
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