2hzm
From Proteopedia
(New page: 200px<br /><applet load="2hzm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hzm, resolution 2.4Å" /> '''Structure of the Medi...) |
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| - | [[Image:2hzm.jpg|left|200px]]<br /><applet load="2hzm" size=" | + | [[Image:2hzm.jpg|left|200px]]<br /><applet load="2hzm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2hzm, resolution 2.4Å" /> | caption="2hzm, resolution 2.4Å" /> | ||
'''Structure of the Mediator head subcomplex Med18/20'''<br /> | '''Structure of the Mediator head subcomplex Med18/20'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Mediator head module stimulates basal RNA polymerase II (Pol II) | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2HZM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2HZM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HZM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: channel]] | [[Category: channel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:47:34 2008'' |
Revision as of 15:47, 21 February 2008
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Structure of the Mediator head subcomplex Med18/20
Overview
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.
About this Structure
2HZM is a Protein complex structure of sequences from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.
Reference
Structure and TBP binding of the Mediator head subcomplex Med8-Med18-Med20., Lariviere L, Geiger S, Hoeppner S, Rother S, Strasser K, Cramer P, Nat Struct Mol Biol. 2006 Oct;13(10):895-901. Epub 2006 Sep 10. PMID:16964259
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