8VLJ
Crystal structure of the cacodylate-bound yeast cytosine deaminase (closed form)
Summary for 8VLJ
| Entry DOI | 10.2210/pdb8vlj/pdb |
| Descriptor | Cytosine deaminase, CACODYLATE ION, 1,2-ETHANEDIOL, ... (6 entities in total) |
| Functional Keywords | cytosine deaminase, resistance, heterodimer, antifungal protein |
| Biological source | Saccharomyces cerevisiae (brewer's yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 36176.52 |
| Authors | Picard, M.-E.,Grenier, J.,Despres, P.C.,Dube, A.K.,Landry, C.R.,Shi, R. (deposition date: 2024-01-11, release date: 2024-08-21, Last modification date: 2024-09-04) |
| Primary citation | Despres, P.C.,Dube, A.K.,Picard, M.E.,Grenier, J.,Shi, R.,Landry, C.R. Compensatory mutations potentiate constructive neutral evolution by gene duplication. Science, 385:770-775, 2024 Cited by PubMed Abstract: The functions of proteins generally depend on their assembly into complexes. During evolution, some complexes have transitioned from homomers encoded by a single gene to heteromers encoded by duplicate genes. This transition could occur without adaptive evolution through intermolecular compensatory mutations. Here, we experimentally duplicated and evolved a homodimeric enzyme to determine whether and how this could happen. We identified hundreds of deleterious mutations that inactivate individual homodimers but produce functional enzymes when coexpressed as duplicated proteins that heterodimerize. The structure of one such heteromer reveals how both losses of function are buffered through the introduction of asymmetry in the complex that allows them to subfunctionalize. Constructive neutral evolution can thus occur by gene duplication followed by only one deleterious mutation per duplicate. PubMed: 39146405DOI: 10.1126/science.ado5719 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.39 Å) |
Structure validation
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