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Structural Protein Function

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
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Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates

Published on: February 27, 2016

Structural and functional analysis of human SIRT1.

Andrew M Davenport¹, Ferdinand M Huber¹, André Hoelz¹

¹Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA.

Journal of Molecular Biology

|October 15, 2013

Summary

Structural insights reveal how the C-terminal regulatory segment (CTR) of SIRT1, a key deacetylase, inhibits its activity. Understanding this interaction is crucial for cellular process regulation.

Keywords:

ADPR GST MALS SEC SSRL Sir2 Stanford Synchrotron Radiation Lightsource X-ray crystallography adenosine diphosphoribose conformational plasticity enzyme peptide substrate interaction enzyme regulation glutathione S-transferase multiangle light scattering mutational analysis silent information regulator 2 size-exclusion chromatography

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Area of Science:

Biochemistry
Structural Biology
Molecular Biology

Background:

Sirtuin 1 (SIRT1) is a crucial NAD(+)-dependent deacetylase involved in diverse cellular functions.
SIRT1 activity is uniquely regulated by its C-terminal regulatory segment (CTR).

Purpose of the Study:

To elucidate the structural mechanisms underlying SIRT1 regulation by its CTR.
To characterize the interaction between the SIRT1 catalytic domain and the CTR.

Main Methods:

X-ray crystallography to determine the structures of the human SIRT1 catalytic domain.
Biochemical analyses to identify key residues and functional roles.

Main Results:

Crystal structures reveal open apo and closed cofactor-bound conformations of the SIRT1 catalytic domain.
The CTR forms a β hairpin that binds to a hydrophobic surface, inhibiting SIRT1 activity.
Key active site residues and inhibitory features of the CTR were identified.

Conclusions:

The CTR plays an inhibitory role in SIRT1 regulation through specific structural interactions.
These findings provide a molecular basis for understanding SIRT1 function and regulation.