Crystal structures of the mitochondrial deacylase Sirtuin 4 reveal isoform-specific acyl recognition and regulation features

Martin Pannek; Zeljko Simic; Matthew Fuszard; Marat Meleshin; Dante Rotili; Antonello Mai; Mike Schutkowski; Clemens Steegborn

doi:10.1038/s41467-017-01701-2

Nature Communications (Nov 2017)

Crystal structures of the mitochondrial deacylase Sirtuin 4 reveal isoform-specific acyl recognition and regulation features

Martin Pannek,
Zeljko Simic,
Matthew Fuszard,
Marat Meleshin,
Dante Rotili,
Antonello Mai,
Mike Schutkowski,
Clemens Steegborn

Affiliations

Martin Pannek: Department of Biochemistry, University of Bayreuth
Zeljko Simic: Department of Enzymology, Institute of Biochemistry and Biotechnology, Martin-Luther-University Halle-Wittenberg
Matthew Fuszard: Department of Biochemistry, University of Bayreuth
Marat Meleshin: Department of Enzymology, Institute of Biochemistry and Biotechnology, Martin-Luther-University Halle-Wittenberg
Dante Rotili: Department of Chemistry and Technologies of Drugs, Pasteur Institute Italy, Cenci-Bolognetti Foundation, Sapienza University of Rome
Antonello Mai: Department of Chemistry and Technologies of Drugs, Pasteur Institute Italy, Cenci-Bolognetti Foundation, Sapienza University of Rome
Mike Schutkowski: Department of Enzymology, Institute of Biochemistry and Biotechnology, Martin-Luther-University Halle-Wittenberg
Clemens Steegborn: Department of Biochemistry, University of Bayreuth

DOI: https://doi.org/10.1038/s41467-017-01701-2
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 13

Abstract

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Sirtuins are NAD+-dependent protein lysine deacylases that act as metabolic regulators and are linked to aging-related diseases. Here the authors present the Sirt4 crystal structure and show that the enzyme has dehydroxymethylglutarylation activity and is regulated by NADH.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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