1q1a

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[[Image:1q1a.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1q1a", creates the "Structure Box" on the page.
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{{STRUCTURE_1q1a| PDB=1q1a | SCENE= }}
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|RELATEDENTRY=[[1q14|1Q14]], [[1q17|1Q17]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q1a OCA], [http://www.ebi.ac.uk/pdbsum/1q1a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q1a RCSB]</span>
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'''Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide'''
'''Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide'''
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[[Category: Marmorstein, R.]]
[[Category: Marmorstein, R.]]
[[Category: Zhao, K.]]
[[Category: Zhao, K.]]
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[[Category: 2'-o-adp ribose,]]
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[[Category: 2'-o-adp ribose]]
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[[Category: histone deacetylase]]
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[[Category: Histone deacetylase]]
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[[Category: ternary complex]]
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[[Category: Ternary complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:44:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:07:27 2008''
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Revision as of 02:44, 3 May 2008

Template:STRUCTURE 1q1a

Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide


Overview

Sir2 proteins are NAD(+)-dependant protein deactylases that have been implicated in playing roles in gene silencing, DNA repair, genome stability, longevity, metabolism, and cell physiology. To define the mechanism of Sir2 activity, we report the 1.5 A crystal structure of the yeast Hst2 (yHst2) Sir2 protein in ternary complex with 2'-O-acetyl ADP ribose and an acetylated histone H4 peptide. The structure captures both ligands meeting within an enclosed tunnel between the small and large domains of the catalytic protein core and permits the assignment of a detailed catalytic mechanism for the Sir2 proteins that is consistent with solution and enzymatic studies. Comparison of the ternary complex with the yHst2/NAD(+) complex, also reported here, and nascent yHst2 structure also reveals that NAD(+) binding accompanies intramolecular loop rearrangement for more stable NAD(+) and acetyl-lysine binding, and that acetyl-lysine peptide binding induces a trimer-monomer protein transition involving nonconserved Sir2 residues.

About this Structure

1Q1A is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide., Zhao K, Chai X, Marmorstein R, Structure. 2003 Nov;11(11):1403-11. PMID:14604530 Page seeded by OCA on Sat May 3 05:44:38 2008

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