1qsn: Difference between revisions

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[[Image:1qsn.gif|left|200px]]
{{Seed}}
[[Image:1qsn.png|left|200px]]


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{{STRUCTURE_1qsn|  PDB=1qsn  |  SCENE=  }}  
{{STRUCTURE_1qsn|  PDB=1qsn  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND COENZYME A AND HISTONE H3 PEPTIDE'''
===CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND COENZYME A AND HISTONE H3 PEPTIDE===




==Overview==
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Gene activation is a highly regulated process that requires the coordinated action of proteins to relieve chromatin repression and to promote transcriptional activation. Nuclear histone acetyltransferase (HAT) enzymes provide a mechanistic link between chromatin destabilization and gene activation by acetylating the epsilon-amino group of specific lysine residues within the aminoterminal tails of core histones to facilitate access to DNA by transcriptional activators. Here we report the high-resolution crystal structure of the HAT domain of Tetrahymena GCN5 (tGCN5) bound with both its physiologically relevant ligands, coenzyme A (CoA) and a histone H3 peptide, and the structures of nascent tGCN5 and a tGCN5/acetyl-CoA complex. Our structural data reveal histone-binding specificity for a random-coil structure containing a G-K-X-P recognition sequence, and show that CoA is essential for reorienting the enzyme for histone binding. Catalysis appears to involve water-mediated proton extraction from the substrate lysine by a glutamic acid general base and a backbone amide that stabilizes the transition-state reaction intermediate. Comparison with related N-acetyltransferases indicates a conserved structural framework for CoA binding and catalysis, and structural variability in regions associated with substrate-specific binding.
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{{ABSTRACT_PUBMED_10485713}}


==About this Structure==
==About this Structure==
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[[Category: Histone acetyltransferase]]
[[Category: Histone acetyltransferase]]
[[Category: Ternary complex]]
[[Category: Ternary complex]]
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Revision as of 02:45, 29 July 2008

File:1qsn.png

Template:STRUCTURE 1qsn

CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND COENZYME A AND HISTONE H3 PEPTIDE

Template:ABSTRACT PUBMED 10485713

About this Structure

1QSN is a Protein complex structure of sequences from Saccharomyces cerevisiae and Tetrahymena thermophila. Full crystallographic information is available from OCA.

Reference

Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide., Rojas JR, Trievel RC, Zhou J, Mo Y, Li X, Berger SL, Allis CD, Marmorstein R, Nature. 1999 Sep 2;401(6748):93-8. PMID:10485713

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