1mjb
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(New page: 200px<br /><applet load="1mjb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mjb, resolution 2.5Å" /> '''Crystal structure of ...)
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Revision as of 19:19, 20 November 2007
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Crystal structure of yeast Esa1 histone acetyltransferase E338Q mutant complexed with acetyl coenzyme A
Overview
Yeast ESA1 is a member of the MYST subfamily of histone acetyltransferases, (HATs), which use acetyl-coenzyme A (CoA) to acetylate specific Lys, residues within histones to regulate gene expression. The structure of an, ESA1-CoA complex reveals structural similarity to the catalytic core of, the GCN5/PCAF subfamily of HAT proteins. Here we report additional, structural and functional studies on ESA1 that demonstrate that histone, acetylation proceeds through an acetyl-cysteine enzyme intermediate. This, Cys residue is strictly conserved within the MYST members, suggesting a, common mode of catalysis by this HAT subfamily. However, this mode of, catalysis differs dramatically from the GCN5/PCAF subfamily, which mediate, direct nucleophilic attack of the acetyl-CoA cofactor by the, enzyme-deprotonated substrate lysine of the histone. These results, demonstrate that different HAT subfamilies can use distinct catalytic, mechanisms, which have implications for their distinct biological roles, and for the development of HAT-specific inhibitors.
About this Structure
1MJB is a Single protein structure of sequence from Saccharomyces cerevisiae with ACO as ligand. Full crystallographic information is available from OCA.
Reference
The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate., Yan Y, Harper S, Speicher DW, Marmorstein R, Nat Struct Biol. 2002 Nov;9(11):862-9. PMID:12368900
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