1ygh: Difference between revisions
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New page: left|200px<br /><applet load="1ygh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ygh, resolution 1.90Å" /> '''HAT DOMAIN OF GCN5 F... |
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[[Image:1ygh.jpg|left|200px]]<br /><applet load="1ygh" size=" | [[Image:1ygh.jpg|left|200px]]<br /><applet load="1ygh" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ygh, resolution 1.90Å" /> | caption="1ygh, resolution 1.90Å" /> | ||
'''HAT DOMAIN OF GCN5 FROM SACCHAROMYCES CEREVISIAE'''<br /> | '''HAT DOMAIN OF GCN5 FROM SACCHAROMYCES CEREVISIAE'''<br /> | ||
==Overview== | ==Overview== | ||
The yeast GCN5 (yGCN5) transcriptional coactivator functions as a histone | 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== | ==About this Structure== | ||
1YGH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] Full crystallographic information is available from [http:// | 1YGH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YGH OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Allis, C | [[Category: Allis, C D.]] | ||
[[Category: Berger, S | [[Category: Berger, S L.]] | ||
[[Category: Marmorstein, R.]] | [[Category: Marmorstein, R.]] | ||
[[Category: Rojas, J | [[Category: Rojas, J R.]] | ||
[[Category: Sterner, D | [[Category: Sterner, D E.]] | ||
[[Category: Trievel, R | [[Category: Trievel, R C.]] | ||
[[Category: Venkataramani, R.]] | [[Category: Venkataramani, R.]] | ||
[[Category: Wang, L.]] | [[Category: Wang, L.]] | ||
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[[Category: transcriptional regulation]] | [[Category: transcriptional regulation]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:05:06 2008'' | ||
