1mj9: Difference between revisions

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[[Image:1mj9.jpg|left|200px]]
{{Seed}}
[[Image:1mj9.png|left|200px]]


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{{STRUCTURE_1mj9|  PDB=1mj9  |  SCENE=  }}  
{{STRUCTURE_1mj9|  PDB=1mj9  |  SCENE=  }}  


'''Crystal structure of yeast Esa1(C304S) mutant complexed with Coenzyme A'''
===Crystal structure of yeast Esa1(C304S) mutant complexed with Coenzyme A===




==Overview==
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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.
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{{ABSTRACT_PUBMED_12368900}}


==About this Structure==
==About this Structure==
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[[Category: Histone acetyltransferase]]
[[Category: Histone acetyltransferase]]
[[Category: Myst]]
[[Category: Myst]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:05:56 2008''

Revision as of 21:05, 2 July 2008

File:1mj9.png

Template:STRUCTURE 1mj9

Crystal structure of yeast Esa1(C304S) mutant complexed with Coenzyme A

Template:ABSTRACT PUBMED 12368900

About this Structure

1MJ9 is a Single protein structure of sequence from Saccharomyces cerevisiae. 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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