3FBI
Structure of the Mediator submodule Med7N/31
Summary for 3FBI
| Entry DOI | 10.2210/pdb3fbi/pdb |
| Related | 3FBN |
| Descriptor | Mediator of RNA polymerase II transcription subunit 7, Mediator of RNA polymerase II transcription subunit 31 (3 entities in total) |
| Functional Keywords | proline-rich stretches, right-handed four-helix bundle, protein-protein complex, nucleus, transcription, transcription regulation, activator |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Cellular location | Nucleus: Q08278 P38633 |
| Total number of polymer chains | 4 |
| Total formula weight | 49279.69 |
| Authors | Koschubs, T.,Seizl, M.,Lariviere, L.,Kurth, F.,Baumli, S.,Martin, D.E.,Cramer, P. (deposition date: 2008-11-19, release date: 2008-12-16, Last modification date: 2024-10-16) |
| Primary citation | Koschubs, T.,Seizl, M.,Lariviere, L.,Kurth, F.,Baumli, S.,Martin, D.E.,Cramer, P. Identification, structure, and functional requirement of the Mediator submodule Med7N/31 Embo J., 28:69-80, 2009 Cited by PubMed Abstract: Mediator is a modular multiprotein complex required for regulated transcription by RNA polymerase (Pol) II. Here, we show that the middle module of the Mediator core contains a submodule of unique structure and function that comprises the N-terminal part of subunit Med7 (Med7N) and the highly conserved subunit Med31 (Soh1). The Med7N/31 submodule shows a conserved novel fold, with two proline-rich stretches in Med7N wrapping around the right-handed four-helix bundle of Med31. In vitro, Med7N/31 is required for activated transcription and can act in trans when added exogenously. In vivo, Med7N/31 has a predominantly positive function on the expression of a specific subset of genes, including genes involved in methionine metabolism and iron transport. Comparative phenotyping and transcriptome profiling identify specific and overlapping functions of different Mediator submodules. PubMed: 19057509DOI: 10.1038/emboj.2008.254 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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