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5U0S

Cryo-EM structure of the Mediator-RNAPII complex

Summary for 5U0S
Entry DOI10.2210/pdb5u0s/pdb
Related5U0P
EMDB information8479 8480
DescriptorMediator complex subunit 6, Mediator complex subunit 7, Mediator complex subunit 21, ... (28 entities in total)
Functional Keywordstranscriptional, transcription, mediator, srb, rna polymerase ii, rna, pol2, activation, complex, transcription-transferase complex, transcription/transferase
Biological sourceSchizosaccharomyces pombe (Fission yeast)
More
Total number of polymer chains28
Total formula weight953381.99
Authors
Tsai, K.-L.,Yu, X.,Gopalan, S.,Chao, T.-C.,Zhang, Y.,Florens, L.,Washburn, M.P.,Murakami, K.,Conaway, R.C.,Conaway, J.W.,Asturias, F. (deposition date: 2016-11-26, release date: 2017-03-08, Last modification date: 2024-11-20)
Primary citationTsai, K.L.,Yu, X.,Gopalan, S.,Chao, T.C.,Zhang, Y.,Florens, L.,Washburn, M.P.,Murakami, K.,Conaway, R.C.,Conaway, J.W.,Asturias, F.J.
Mediator structure and rearrangements required for holoenzyme formation.
Nature, 544:196-201, 2017
Cited by
PubMed Abstract: The conserved Mediator co-activator complex has an essential role in the regulation of RNA polymerase II transcription in all eukaryotes. Understanding the structure and interactions of Mediator is crucial for determining how the complex influences transcription initiation and conveys regulatory information to the basal transcription machinery. Here we present a 4.4 Å resolution cryo-electron microscopy map of Schizosaccharomyces pombe Mediator in which conserved Mediator subunits are individually resolved. The essential Med14 subunit works as a central backbone that connects the Mediator head, middle and tail modules. Comparison with a 7.8 Å resolution cryo-electron microscopy map of a Mediator-RNA polymerase II holoenzyme reveals that changes in the structure of Med14 facilitate a large-scale Mediator rearrangement that is essential for holoenzyme formation. Our study suggests that access to different conformations and crosstalk between structural elements are essential for the Mediator regulation mechanism, and could explain the capacity of the complex to integrate multiple regulatory signals.
PubMed: 28241144
DOI: 10.1038/nature21393
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (7.8 Å)
Structure validation

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