1pua

Crystal Structure of Tetrahymena GCN5 with Bound Coenzyme A and a Phosphorylated, 19-residue Histone H3 peptide

spinqualitylabelsall models 1pua, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1pua is a 2 chain structure with sequence from Saccharomyces cerevisiae and Tetrahymena thermophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: COA, SEP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q27198_TETTH Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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