1CM0

CRYSTAL STRUCTURE OF THE PCAF/COENZYME-A COMPLEX

Summary for 1CM0

• Entry DOI: 10.2210/pdb1cm0/pdb
• Descriptor: P300/CBP ASSOCIATING FACTOR, COENZYME A (3 entities in total)
• Functional Keywords: p300/cbp associated factor, coenzyme a, acetyltransferase, coactivator, signaling protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 40552.85

Authors

Clements, A.,Rojas, J.R.,Trievel, R.C.,Wang, L.,Berger, S.L.,Marmorstein, R. (deposition date: 1999-05-12, release date: 1999-07-06, Last modification date: 2024-04-03)

Primary citation

Clements, A.,Rojas, J.R.,Trievel, R.C.,Wang, L.,Berger, S.L.,Marmorstein, R.
Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A.
EMBO J., 18:3521-3532, 1999

PubMed Abstract: 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.

PubMed: 10393169
DOI: 10.1093/emboj/18.13.3521

Experimental method

X-RAY DIFFRACTION (2.3 Å)