1cm0
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CRYSTAL STRUCTURE OF THE PCAF/COENZYME-A COMPLEX
OverviewOverview
The human p300/CBP-associating factor, PCAF, mediates transcriptional, activation through its ability to acetylate nucleosomal histone substrates, as well as transcriptional activators such as p53. We have determined the, 2.3 A crystal structure of the histone acetyltransferase (HAT) domain of, PCAF bound to coenzyme A. The structure reveals a central protein core, associated with coenzyme A binding and a pronounced cleft that sits over, the protein core and is flanked on opposite sides by the N- and C-terminal, protein segments. A correlation of the structure with the extensive, mutagenesis data for PCAF and the homologous yeast GCN5 protein implicates, the cleft and the N- and C-terminal protein segments as playing an, important role in histone substrate binding, and a glutamate residue in, the protein core as playing an essential catalytic role. A structural, comparison with the coenzyme-bound forms of the related, N-acetyltransferases, HAT1 (yeast histone acetyltransferase 1) and SmAAT, (Serratia marcescens aminoglycoside 3-N-acetyltransferase), suggests the, mode of substrate binding and catalysis by these enzymes and establishes a, paradigm for understanding the structure-function relationships of other, enzymes that acetylate histones and transcriptional regulators to promote, activated transcription.
About this StructureAbout this Structure
1CM0 is a Single protein structure of sequence from Homo sapiens with COA as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A., Clements A, Rojas JR, Trievel RC, Wang L, Berger SL, Marmorstein R, EMBO J. 1999 Jul 1;18(13):3521-32. PMID:10393169
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