1pu9: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1pu9.gif|left|200px]]
{{Seed}}
[[Image:1pu9.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1pu9|  PDB=1pu9  |  SCENE=  }}  
{{STRUCTURE_1pu9|  PDB=1pu9  |  SCENE=  }}  


'''Crystal Structure of Tetrahymena GCN5 with Bound Coenzyme A and a 19-residue Histone H3 Peptide'''
===Crystal Structure of Tetrahymena GCN5 with Bound Coenzyme A and a 19-residue Histone H3 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.
The line below this paragraph, {{ABSTRACT_PUBMED_14536085}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 14536085 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_14536085}}


==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Histone acetyltransferase]]
[[Category: Histone acetyltransferase]]
[[Category: Ternary complex]]
[[Category: Ternary complex]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:29:26 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:26:54 2008''