ISDA: 3R84

Deposition Date 2011-03-23

Release Date 2011-04-27

Last Version Date 2024-11-20

Entry Detail

PDB ID:

3R84

Keywords:

TRANSCRIPTION

Title:

Structure of the Mediator head subcomplex Med11/22

Biological Source:

Source Organism(s):

Saccharomyces cerevisiae (Taxon ID: 4932)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

2.05 Å

R-Value Free:

0.20

R-Value Work:

0.16

R-Value Observed:

0.17

Space Group:

P 21 21 2

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Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Mediator of RNA polymerase II
Gene (Uniprot):MED11
Chain IDs:A, C, E, G, I, K, M, O, Q, S, U, W
Chain Length:86
Number of Molecules:12
Biological Source:Saccharomyces cerevisiae

UniProt ID:Q99278 Pfam ID:PF10280

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Mediator of RNA polymerase II
Gene (Uniprot):SRB6
Mutagens:M27I
Chain IDs:B, D, F, H, J, L, N, P, R, T, V, X
Chain Length:92
Number of Molecules:12
Biological Source:Saccharomyces cerevisiae

UniProt ID:P32570 Pfam ID:PF06179

Modified Residue

Compound ID	Chain ID	Parent Comp ID	Details	2D Image
MSE	A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X	MET	SELENOMETHIONINE

Primary Citation

Mediator head subcomplex Med11/22 contains a common helix bundle building block with a specific function in transcription initiation complex stabilization.

Seizl, M, Lariviere, L, Pfaffeneder, T, Wenzeck, L, Cramer, P.Show

Nucleic Acids Res. 39 6291 6304 (2011)

PMID: 21498544 DOI: 10.1093/nar/gkr229

Abstact

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.

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Primary Citation of related structures

Abstact

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