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American Society for Microbiology, Journal of Virology, 21(79), p. 13685-13693, 2005

DOI: 10.1128/jvi.79.21.13685-13693.2005

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A Norovirus Protease Structure Provides Insights into Active and Substrate Binding Site Integrity†

Journal article published in 2005 by Kentaro Nakamura, Yuichi Someya, Takashi Kumasaka ORCID, Go Ueno, Masaki Yamamoto, Takao Sato, Naokazu Takeda, Tatsuo Miyamura, Nobuo Tanaka
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

ABSTRACT Norovirus 3C-like proteases are crucial to proteolytic processing of norovirus polyproteins. We determined the crystal structure of the 3C-like protease from Chiba virus, a norovirus, at 2.8-Å resolution. An active site including Cys139 and His30 is present, as is a hydrogen bond network that stabilizes the active site conformation. In the oxyanion hole backbone, a structural difference was observed probably upon substrate binding. A peptide substrate/enzyme model shows that several interactions between the two components are critical for substrate binding and that the S1 and S2 sites appropriately accommodate the substrate P1 and P2 residues, respectively. Knowledge of the structure and a previous mutagenesis study allow us to correlate proteolysis and structure.