9F76
CryoEM structure of human Mediator subunit Med23
Summary for 9F76
| Entry DOI | 10.2210/pdb9f76/pdb |
| EMDB information | 50247 |
| Descriptor | Mediator of RNA polymerase II transcription subunit 23 (1 entity in total) |
| Functional Keywords | mediator, med23, transcription, human |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 158294.89 |
| Authors | |
| Primary citation | Monte, D.,Lens, Z.,Dewitte, F.,Fislage, M.,Aumercier, M.,Verger, A.,Villeret, V. Structural basis of human Mediator recruitment by the phosphorylated transcription factor Elk-1. Nat Commun, 16:3772-3772, 2025 Cited by PubMed Abstract: One function of Mediator complex subunit MED23 is to mediate transcriptional activation by the phosphorylated transcription factor Elk-1, in response to the Ras-MAPK signaling pathway. Using cryogenic electron microscopy, we solve a 3.0 Å structure of human MED23 complexed with the phosphorylated activation domain of Elk-1. Elk-1 binds to MED23 via a hydrophobic sequence PSIHFWSTLSP containing one phosphorylated residue (S383), which forms a tight turn around the central Phenylalanine. Binding of Elk-1 induces allosteric changes in MED23 that propagate to the opposite face of the subunit, resulting in the dynamic behavior of a 19-residue segment, which alters the molecular surface of MED23. We design a specific MED23 mutation (G382F) that disrupts Elk--1 binding and consequently impairs Elk-1-dependent serum-induced activation of target genes in the Ras-Raf-MEK-ERK signaling pathway. The structure provides molecular details and insights into a Mediator subunit-transcription factor interface. PubMed: 40263353DOI: 10.1038/s41467-025-59014-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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