5gcn

CATALYTIC DOMAIN OF TETRAHYMENA GCN5 HISTONE ACETYLTRANSFERASE IN COMPLEX WITH COENZYME A

spinqualitylabelsall models 5gcn Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5gcn is a 1 chain structure with sequence from Tetrahymena thermophila. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: COA 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 Gene transcription requires the release of inactive DNA from its packaging of histone proteins. Following the discovery of the first transcription-associated histone acetyltransferase, tetrahymena GCN5, it was shown that yeast GCN5 is recruited to the promoter and causes hyper-acetylation of histones and transcriptional activation of target genes, establishing a direct connection between histone acetylation and transcriptional activation. Many other important transcription regulators have been found to have histone acetyltransferase activity, including TAFII230/250, p300/CBP and its associated factor PCAF. Here we present the solution structure of the catalytic domain of tGCN5 (residues 47-210) in complex with coenzyme A. The structure contains two domains; the amino-terminal domain is similar to those of other GCN5-related N-acetyltransferases but the carboxy-terminal domain is not. Coenzyme A binds in a deep hydrophobic pocket between the two domains. Chemical shift changes upon titration with histone H3 peptides indicate a binding site at the domain boundary opposite to the coenzyme A site. The structural data indicate a single-step acetyl-transfer reaction mechanism catalysed by a hydrogen bond to the backbone amide group of leucine 126 and the side-chain carboxyl group of a conserved acidic residue. Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A.,Lin Y, Fletcher CM, Zhou J, Allis CD, Wagner G Nature. 1999 Jul 1;400(6739):86-9. PMID:10403255 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Histone acetyltransferase 3D structures

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