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Reaction Mechanism of Mono-ADP-Ribosyltransferase Based on Structures of the Complex of Enzyme and Substrate Protein

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Endogenous ADP-Ribosylation

Part of the book series: Current Topics in Microbiology and Immunology ((CT MICROBIOLOGY,volume 384))

Abstract

Mono-ADP-ribosylation is a post-translational protein modification catalyzed by bacterial toxins and exoenzymes that function as ADP-ribosyltransferases. Despite the importance of this modification, the reaction mechanism remains poorly understood due to a lack of information on the crystal structure of these enzymes in complex with a substrate protein. Recently, the structures of two such complexes became available, which shed new light on the mechanisms of mono-ADP-ribosylation. In this review, we consider the reaction mechanism based on the structures of ADP-ribosyltransferases in complex with a substrate protein.

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Acknowledgments

H.T. appreciates Masahiro Nagahama, Masataka Oda, and Jun Sakurai, who support our work on the structure of ART, and Nobuhiko Katunuma for his continuous research support. This work was supported in part by a Strategic Research Foundation Grant-aided Project for Private Universities and Grant-in-Aid for Scientific Research on Innovative Areas, MEXT/JSPS KAKENHI Grant Number: 25121733 of Japan.

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  1. Faculty of Life Sciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto, 603-8555, Japan

    Hideaki Tsuge & Toshiharu Tsurumura

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  1. Hideaki Tsuge
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  2. Toshiharu Tsurumura
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Correspondence to Hideaki Tsuge .

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  1. Institute of Immunology, University Medical Center, Hamburg, Germany

    Friedrich Koch-Nolte

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Tsuge, H., Tsurumura, T. (2014). Reaction Mechanism of Mono-ADP-Ribosyltransferase Based on Structures of the Complex of Enzyme and Substrate Protein. In: Koch-Nolte, F. (eds) Endogenous ADP-Ribosylation. Current Topics in Microbiology and Immunology, vol 384. Springer, Cham. https://doi.org/10.1007/82_2014_415

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