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2HZS

Structure of the Mediator head submodule Med8C/18/20

Summary for 2HZS
Entry DOI10.2210/pdb2hzs/pdb
Related1YKE 1YKH 1ZP2 2HZM
DescriptorRNA 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 Keywordsbeta barrel, channel, helix, transcription
Biological sourceSaccharomyces cerevisiae (baker's yeast)
More
Cellular locationNucleus: P34162 P32585
Nucleus (Probable): P38304
Total number of polymer chains12
Total formula weight240871.41
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 citationLariviere, 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: 16964259
DOI: 10.1038/nsmb1143
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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