1q2c
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(New page: 200px<br /><applet load="1q2c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q2c, resolution 2.25Å" /> '''Crystal Structure of...)
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Revision as of 01:18, 25 November 2007
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Crystal Structure of Tetrahymena GCN5 With Bound Coenzyme A and a 19-residue Histone H4 Peptide
Overview
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.
About this Structure
1Q2C is a Single protein structure of sequence from Tetrahymena thermophila with COA as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis for histone and phosphohistone binding by the GCN5 histone acetyltransferase., Clements A, Poux AN, Lo WS, Pillus L, Berger SL, Marmorstein R, Mol Cell. 2003 Aug;12(2):461-73. PMID:14536085
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