User:Jamie Abbott/Sandbox1
From Proteopedia
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Revision as of 21:38, 19 April 2011
Contents |
Histone Acetyltransferase GCN5
Histone Acetyltransferase (HAT) GCN5 is a ~94 kD (837 amino acid) protein. It is a nuclear HAT or A-type HAT. Most if not all HATs function in vivo as members of often large multisubunit complexes, many of which were initially characterized as transcriptional regulators.
GCN5 catalyzes the acetylation of specific Lysine residues of histones H3 and H4. Histone acetylation is an important
HAT Domain
The HAT domain of human GCN5 consists of amino acid residues 496-658. This domain is a mixed alpha beta structure with 7 and seven anti-parallel .
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Catalysis
GCN5 catalyzes the transfer of an acetyl group from acetyl coenzyme A () onto the ε-amino group of specific lysine residues present in the amino-terminal tails of each of the core histones resulting in the neutralization of a single positive charge. [1]
Bromo Domain
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References
- ↑ Schuetz A, Bernstein G, Dong A, Antoshenko T, Wu H, Loppnau P, Bochkarev A, Plotnikov AN. Crystal structure of a binary complex between human GCN5 histone acetyltransferase domain and acetyl coenzyme A. Proteins. 2007 Jul 1;68(1):403-7. PMID:17410582 doi:10.1002/prot.21407
