1q2c: Difference between revisions

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[[Image:1q2c.jpg|left|200px]]
{{Seed}}
[[Image:1q2c.png|left|200px]]


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{{STRUCTURE_1q2c|  PDB=1q2c  |  SCENE=  }}  
{{STRUCTURE_1q2c|  PDB=1q2c  |  SCENE=  }}  


'''Crystal Structure of Tetrahymena GCN5 With Bound Coenzyme A and a 19-residue Histone H4 Peptide'''
===Crystal Structure of Tetrahymena GCN5 With Bound Coenzyme A and a 19-residue Histone H4 Peptide===




==Overview==
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Distinct posttranslational modifications on histones occur in specific patterns to mediate certain chromosomal events. For example, on histone H3, phosphorylation at Ser10 can enhance GCN5-mediated Lys14 acetylation to promote transcription. To gain insight into the mechanism underlying this synergism, we determined the structure of Tetrahymena GCN5 (tGCN5) and coenzyme A (CoA) bound to unmodified and Ser10-phosphorylated 19 residue histone H3 peptides (H3p19 and H3p19Pi, respectively). The tGCN5/CoA/H3p19 structure reveals that a 12 amino acid core sequence mediates extensive contacts with the protein, providing the structural basis for substrate specificity by the GCN5/PCAF family of histone acetyltransferases. Comparison with the tGCN5/CoA/H3p19Pi structure reveals that phospho-Ser10 and Thr11 mediate significant histone-protein interactions, and nucleate additional interactions distal to the phosphorylation site. Functional studies show that histone H3 Thr11 is necessary for optimal transcription at yGcn5-dependent promoters requiring Ser10 phosphorylation. Together, these studies reveal how one histone modification can modulate another to affect distinct transcriptional signals.
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==About this Structure==
==About this Structure==
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[[Category: Tetrahymena]]
[[Category: Tetrahymena]]
[[Category: X-ray structure]]
[[Category: X-ray structure]]
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