1ygh

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spinqualitylabelsall models 1ygh, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

HAT DOMAIN OF GCN5 FROM SACCHAROMYCES CEREVISIAE

Overview

The yeast GCN5 (yGCN5) transcriptional coactivator functions as a histone, acetyltransferase (HAT) to promote transcriptional activation. Here, we, present the high resolution crystal structure of the HAT domain of yGCN5, and probe the functional importance of a conserved glutamate residue. The, structure reveals a central protein core associated with AcCoA binding, that appears to be structurally conserved among a superfamily of, N-acetyltransferases, including yeast histone acetyltransferase 1 and, Serratia marcescens aminoglycoside 3-N-acetyltransferase. A pronounced, cleft lying above this core, and flanked by N- and C-terminal regions that, show no sequence conservation within N-acetyltransferase enzymes, is, implicated by cross-species conservation and mutagenesis studies to be a, site for histone substrate binding and catalysis. Located at the bottom of, this cleft is a conserved glutamate residue (E173) that is in position to, play an important catalytic role in histone acetylation. Functional, analysis of an E173Q mutant yGCN5 protein implicates glutamate 173 to, function as a general base for catalysis. Together, a correlation of the, yGCN5 structure with functionally debilitating yGCN5 mutations provides a, paradigm for understanding the structure/function relationships of the, growing number of transcriptional regulators that function as histone, acetyltransferase enzymes.

About this Structure

1YGH is a Single protein structure of sequence from Saccharomyces cerevisiae with GOL as ligand. Active as Histone acetyltransferase, with EC number 2.3.1.48 Full crystallographic information is available from OCA.

Reference

Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator., Trievel RC, Rojas JR, Sterner DE, Venkataramani RN, Wang L, Zhou J, Allis CD, Berger SL, Marmorstein R, Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8931-6. PMID:10430873

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