5XW4
Crystal structure of budding yeast Cdc14p (wild type) in the apo state
Summary for 5XW4
| Entry DOI | 10.2210/pdb5xw4/pdb |
| Descriptor | Tyrosine-protein phosphatase CDC14 (2 entities in total) |
| Functional Keywords | phosphatase, cell cycle |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Cellular location | Nucleus, nucleolus: Q00684 |
| Total number of polymer chains | 2 |
| Total formula weight | 95281.66 |
| Authors | Kobayashi, J.,Matsuura, Y. (deposition date: 2017-06-29, release date: 2017-08-09, Last modification date: 2023-11-22) |
| Primary citation | Kobayashi, J.,Matsuura, Y. Structure and dimerization of the catalytic domain of the protein phosphatase Cdc14p, a key regulator of mitotic exit in Saccharomyces cerevisiae Protein Sci., 26:2105-2112, 2017 Cited by PubMed Abstract: In the budding yeast Saccharomyces cerevisiae, the protein phosphatase Cdc14p orchestrates various events essential for mitotic exit. We have determined the X-ray crystal structures at 1.85 Å resolution of the catalytic domain of Cdc14p in both the apo state, and as a complex with S160-phosphorylated Swi6p peptide. Each asymmetric unit contains two Cdc14p chains arranged in an intimately associated homodimer, consistent with its oligomeric state in solution. The dimerization interface is located on the backside of the substrate-binding cleft. Structure-based mutational analyses indicate that the dimerization of Cdc14p is required for normal growth of yeast cells. PubMed: 28758351DOI: 10.1002/pro.3244 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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