2h2d

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{{STRUCTURE_2h2d| PDB=2h2d | SCENE= }}
{{STRUCTURE_2h2d| PDB=2h2d | SCENE= }}
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'''The Structural Basis for Sirtuin Substrate Affinity'''
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===The Structural Basis for Sirtuin Substrate Affinity===
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==Overview==
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Sirtuins comprise a family of enzymes that catalyze the deacetylation of acetyllysine side chains in a reaction that consumes NAD+. Although several crystal structures of sirtuins bound to non-native acetyl peptides have been determined, relatively little about how sirtuins discriminate among different substrates is understood. We have carried out a systematic structural and thermodynamic analysis of several peptides bound to a single sirtuin, the Sir2 homologue from Thermatoga maritima (Sir2Tm). We report structures of five different forms of Sir2Tm: two forms bound to the p53 C-terminal tail in the acetylated and unacetylated states, two forms bound to putative acetyl peptide substrates derived from the structured domains of histones H3 and H4, and one form bound to polypropylene glycol (PPG), which resembles the apoenzyme. The structures reveal previously unobserved complementary side chain interactions between Sir2Tm and the first residue N-terminal to the acetyllysine (position -1) and the second residue C-terminal to the acetyllysine (position +2). Isothermal titration calorimetry was used to compare binding constants between wild-type and mutant forms of Sir2Tm and between additional acetyl peptide substrates with substitutions at positions -1 and +2. The results are consistent with a model in which peptide positions -1 and +2 play a significant role in sirtuin substrate binding. This model provides a framework for identifying sirtuin substrates.
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(as it appears on PubMed at http://www.pubmed.gov), where 16768447 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16768447}}
==About this Structure==
==About this Structure==
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[[Category: Sirt1]]
[[Category: Sirt1]]
[[Category: Sirtuin]]
[[Category: Sirtuin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:47:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:47:50 2008''

Revision as of 21:47, 28 July 2008

Image:2h2d.png

Template:STRUCTURE 2h2d

The Structural Basis for Sirtuin Substrate Affinity

Template:ABSTRACT PUBMED 16768447

About this Structure

2H2D is a Protein complex structure of sequences from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

The structural basis of sirtuin substrate affinity., Cosgrove MS, Bever K, Avalos JL, Muhammad S, Zhang X, Wolberger C, Biochemistry. 2006 Jun 20;45(24):7511-21. PMID:16768447

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