1n72
|
Structure and Ligand of a Histone Acetyltransferase Bromodomain
OverviewOverview
Histone acetylation is important in chromatin remodelling and gene, activation. Nearly all known histone-acetyltransferase (HAT)-associated, transcriptional co-activators contain bromodomains, which are, approximately 110-amino-acid modules found in many chromatin-associated, proteins. Despite the wide occurrence of these bromodomains, their, three-dimensional structure and binding partners remain unknown. Here we, report the solution structure of the bromodomain of the HAT co-activator, P/CAF (p300/CBP-associated factor). The structure reveals an unusual, left-handed up-and-down four-helix bundle. In addition, we show by a, combination of structural and site-directed mutagenesis studies that, bromodomains can interact specifically with acetylated lysine, making them, the first known protein modules to do so. The nature of the recognition of, acetyl-lysine by the P/CAF bromodomain is similar to that of acetyl-CoA by, histone acetyltransferase. Thus, the bromodomain is functionally linked to, the HAT activity of co-activators in the regulation of gene transcription.
About this StructureAbout this Structure
1N72 is a Single protein structure of sequence from Homo sapiens. This structure superseeds the now removed PDB entry 1B91. Active as Histone acetyltransferase, with EC number 2.3.1.48 Full crystallographic information is available from OCA.
ReferenceReference
Structure and ligand of a histone acetyltransferase bromodomain., Dhalluin C, Carlson JE, Zeng L, He C, Aggarwal AK, Zhou MM, Nature. 1999 Jun 3;399(6735):491-6. PMID:10365964
Page seeded by OCA on Mon Nov 12 18:18:35 2007