1ygh
From Proteopedia
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'''HAT DOMAIN OF GCN5 FROM SACCHAROMYCES CEREVISIAE''' | '''HAT DOMAIN OF GCN5 FROM SACCHAROMYCES CEREVISIAE''' | ||
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[[Category: Wang, L.]] | [[Category: Wang, L.]] | ||
[[Category: Zhou, J.]] | [[Category: Zhou, J.]] | ||
| - | [[Category: | + | [[Category: Gcn5 related n-acetyltransferase family]] |
| - | [[Category: | + | [[Category: Histone acetylation]] |
| - | [[Category: | + | [[Category: N-acetyltransferase]] |
| - | [[Category: | + | [[Category: Transcriptional regulation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:17:23 2008'' | |
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Revision as of 13:17, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 16:17:23 2008
Categories: Histone acetyltransferase | Saccharomyces cerevisiae | Single protein | Allis, C D. | Berger, S L. | Marmorstein, R. | Rojas, J R. | Sterner, D E. | Trievel, R C. | Venkataramani, R. | Wang, L. | Zhou, J. | Gcn5 related n-acetyltransferase family | Histone acetylation | N-acetyltransferase | Transcriptional regulation
