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Journal of Virology, November 2005, p. 13685-13693, Vol. 79, No. 21
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.21.13685-13693.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

A Norovirus Protease Structure Provides Insights into Active and Substrate Binding Site Integrity{dagger}

Kentaro Nakamura,1 Yuichi Someya,2 Takashi Kumasaka,1,3* Go Ueno,3 Masaki Yamamoto,3 Takao Sato,1 Naokazu Takeda,2 Tatsuo Miyamura,2 and Nobuo Tanaka1*

Department of Life Science, Tokyo Institute of Technology, Yokohama 226-8501,1 Department of Virology II, National Institute of Infectious Diseases, Shinjuku, Tokyo 162-8640,2 RIKEN Harima Institute/SPring-8, Mikazuki, Hyogo 679-5148, Japan3

Received 11 May 2005/ Accepted 9 August 2005

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.

* Corresponding author. Mailing address: Department of Life Science, Tokyo Institute of Technology, Yokohama 226-8501, Japan. Phone and fax: 81-45-924-5707. E-mail for Takashi Kumasaka: tkumasak{at}bio.titech.ac.jp. E-mail for Nobuo Tanaka: ntanaka{at}bio.titech.ac.jp.

{dagger} Supplemental material for this article may be found at http://jvi.asm.org/.

Journal of Virology, November 2005, p. 13685-13693, Vol. 79, No. 21
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.21.13685-13693.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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