1eqf
From Proteopedia
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|PDB= 1eqf |SIZE=350|CAPTION= <scene name='initialview01'>1eqf</scene>, resolution 2.1Å | |PDB= 1eqf |SIZE=350|CAPTION= <scene name='initialview01'>1eqf</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eqf OCA], [http://www.ebi.ac.uk/pdbsum/1eqf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eqf RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
TFIID is a large multiprotein complex that initiates assembly of the transcription machinery. It is unclear how TFIID recognizes promoters in vivo when templates are nucleosome-bound. Here, it is shown that TAFII250, the largest subunit of TFIID, contains two tandem bromodomain modules that bind selectively to multiply acetylated histone H4 peptides. The 2.1 angstrom crystal structure of the double bromodomain reveals two side-by-side, four-helix bundles with a highly polarized surface charge distribution. Each bundle contains an Nepsilon-acetyllysine binding pocket at its center, which results in a structure ideally suited for recognition of diacetylated histone H4 tails. Thus, TFIID may be targeted to specific chromatin-bound promoters and may play a role in chromatin recognition. | TFIID is a large multiprotein complex that initiates assembly of the transcription machinery. It is unclear how TFIID recognizes promoters in vivo when templates are nucleosome-bound. Here, it is shown that TAFII250, the largest subunit of TFIID, contains two tandem bromodomain modules that bind selectively to multiply acetylated histone H4 peptides. The 2.1 angstrom crystal structure of the double bromodomain reveals two side-by-side, four-helix bundles with a highly polarized surface charge distribution. Each bundle contains an Nepsilon-acetyllysine binding pocket at its center, which results in a structure ideally suited for recognition of diacetylated histone H4 tails. Thus, TFIID may be targeted to specific chromatin-bound promoters and may play a role in chromatin recognition. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Dystonia-Parkinsonism, X-linked OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=313650 313650]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Ladurner, A G.]] | [[Category: Ladurner, A G.]] | ||
[[Category: Tjian, R.]] | [[Category: Tjian, R.]] | ||
| - | [[Category: SO4]] | ||
[[Category: acetylated histone-tail binding protein]] | [[Category: acetylated histone-tail binding protein]] | ||
[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:07:44 2008'' |
Revision as of 17:07, 30 March 2008
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| , resolution 2.1Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE DOUBLE BROMODOMAIN MODULE FROM HUMAN TAFII250
Overview
TFIID is a large multiprotein complex that initiates assembly of the transcription machinery. It is unclear how TFIID recognizes promoters in vivo when templates are nucleosome-bound. Here, it is shown that TAFII250, the largest subunit of TFIID, contains two tandem bromodomain modules that bind selectively to multiply acetylated histone H4 peptides. The 2.1 angstrom crystal structure of the double bromodomain reveals two side-by-side, four-helix bundles with a highly polarized surface charge distribution. Each bundle contains an Nepsilon-acetyllysine binding pocket at its center, which results in a structure ideally suited for recognition of diacetylated histone H4 tails. Thus, TFIID may be targeted to specific chromatin-bound promoters and may play a role in chromatin recognition.
About this Structure
1EQF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure and function of a human TAFII250 double bromodomain module., Jacobson RH, Ladurner AG, King DS, Tjian R, Science. 2000 May 26;288(5470):1422-5. PMID:10827952
Page seeded by OCA on Sun Mar 30 20:07:44 2008
