3R84

Structure of the Mediator head subcomplex Med11/22

Summary for 3R84

• Entry DOI: 10.2210/pdb3r84/pdb
• Descriptor: Mediator of RNA polymerase II transcription subunit 11, Mediator of RNA polymerase II transcription subunit 22 (3 entities in total)
• Functional Keywords: four-helix bundle, transcription, nucleus
• Biological source: Saccharomyces cerevisiae (yeast); More
• Cellular location: Nucleus : Q99278 P32570
• Total number of polymer chains: 24
• Total formula weight: 248589.25

Authors

Seizl, M.,Lariviere, L.,Pfaffenender, T.,Wenzeck, L.,Cramer, P. (deposition date: 2011-03-23, release date: 2011-04-27, Last modification date: 2024-11-20)

Primary citation

Seizl, M.,Lariviere, L.,Pfaffeneder, T.,Wenzeck, L.,Cramer, P.
Mediator head subcomplex Med11/22 contains a common helix bundle building block with a specific function in transcription initiation complex stabilization.
Nucleic Acids Res., 39:6291-6304, 2011

PubMed Abstract: Mediator is a multiprotein co-activator of RNA polymerase (Pol) II transcription. Mediator contains a conserved core that comprises the 'head' and 'middle' modules. We present here a structure-function analysis of the essential Med11/22 heterodimer, a part of the head module. Med11/22 forms a conserved four-helix bundle domain with C-terminal extensions, which bind the central head subunit Med17. A highly conserved patch on the bundle surface is required for stable transcription pre-initiation complex formation on a Pol II promoter in vitro and in vivo and may recruit the general transcription factor TFIIH. The bundle domain fold is also present in the Mediator middle module subcomplex Med7/21 and is predicted in the Mediator heterodimers Med2/3, Med4/9, Med10/14 and Med28/30. The bundle domain thus represents a common building block that has been multiplied and functionally diversified during Mediator evolution in eukaryotes.

PubMed: 21498544
DOI: 10.1093/nar/gkr229

Experimental method

X-RAY DIFFRACTION (2.05 Å)