6ALY
Solution structure of yeast Med15 ABD2 residues 277-368
Summary for 6ALY
| Entry DOI | 10.2210/pdb6aly/pdb |
| NMR Information | BMRB: 30330 |
| Descriptor | Mediator of RNA polymerase II transcription subunit 15 (1 entity in total) |
| Functional Keywords | mediator, transcription activation, helical, abd, med15, gal11, yeast, transcription |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 10525.71 |
| Authors | Tuttle, L.M.,Pacheco, D.,Warfield, L.,Hahn, S.,Klevit, R.E. (deposition date: 2017-08-08, release date: 2018-03-21, Last modification date: 2024-05-15) |
| Primary citation | Tuttle, L.M.,Pacheco, D.,Warfield, L.,Luo, J.,Ranish, J.,Hahn, S.,Klevit, R.E. Gcn4-Mediator Specificity Is Mediated by a Large and Dynamic Fuzzy Protein-Protein Complex. Cell Rep, 22:3251-3264, 2018 Cited by PubMed Abstract: Transcription activation domains (ADs) are inherently disordered proteins that often target multiple coactivator complexes, but the specificity of these interactions is not understood. Efficient transcription activation by yeast Gcn4 requires its tandem ADs and four activator-binding domains (ABDs) on its target, the Mediator subunit Med15. Multiple ABDs are a common feature of coactivator complexes. We find that the large Gcn4-Med15 complex is heterogeneous and contains nearly all possible AD-ABD interactions. Gcn4-Med15 forms via a dynamic fuzzy protein-protein interface, where ADs bind the ABDs in multiple orientations via hydrophobic regions that gain helicity. This combinatorial mechanism allows individual low-affinity and specificity interactions to generate a biologically functional, specific, and higher affinity complex despite lacking a defined protein-protein interface. This binding strategy is likely representative of many activators that target multiple coactivators, as it allows great flexibility in combinations of activators that can cooperate to regulate genes with variable coactivator requirements. PubMed: 29562181DOI: 10.1016/j.celrep.2018.02.097 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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