2HZS
Structure of the Mediator head submodule Med8C/18/20
Summary for 2HZS
Entry DOI | 10.2210/pdb2hzs/pdb |
Related | 1YKE 1YKH 1ZP2 2HZM |
Descriptor | RNA polymerase II mediator complex subunit 20, RNA polymerase II mediator complex subunit 18, RNA polymerase II mediator complex subunit 8, ... (4 entities in total) |
Functional Keywords | beta barrel, channel, helix, transcription |
Biological source | Saccharomyces cerevisiae (baker's yeast) More |
Cellular location | Nucleus: P34162 P32585 Nucleus (Probable): P38304 |
Total number of polymer chains | 12 |
Total formula weight | 240871.41 |
Authors | Lariviere, L.,Geiger, S.,Hoeppner, S.,Rother, S.,Straesser, K.,Cramer, P. (deposition date: 2006-08-09, release date: 2006-09-12, Last modification date: 2023-08-30) |
Primary citation | Lariviere, L.,Geiger, S.,Hoeppner, S.,Rother, S.,Strasser, K.,Cramer, P. Structure and TBP binding of the Mediator head subcomplex Med8-Med18-Med20. Nat.Struct.Mol.Biol., 13:895-901, 2006 Cited by PubMed Abstract: The Mediator head module stimulates basal RNA polymerase II (Pol II) transcription and enables transcriptional regulation. Here we show that the head subunits Med8, Med18 and Med20 form a subcomplex (Med8/18/20) with two submodules. The highly conserved N-terminal domain of Med8 forms one submodule that binds the TATA box-binding protein (TBP) in vitro and is essential in vivo. The second submodule consists of the C-terminal region of Med8 (Med8C), Med18 and Med20. X-ray analysis of this submodule reveals that Med18 and Med20 form related beta-barrel folds. A conserved putative protein-interaction face on the Med8C/18/20 submodule includes sites altered by srb mutations, which counteract defects resulting from Pol II truncation. Our results and published data support a positive role of the Med8/18/20 subcomplex in initiation-complex formation and suggest that the Mediator head contains a multipartite TBP-binding site that can be modulated by transcriptional activators. PubMed: 16964259DOI: 10.1038/nsmb1143 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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