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1wqs

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(New page: 200px<br /><applet load="1wqs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wqs, resolution 2.80&Aring;" /> '''Crystal structure of...)
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Revision as of 22:25, 24 November 2007


1wqs, resolution 2.80Å

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Crystal structure of Norovirus 3C-like protease

Overview

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-A 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.

About this Structure

1WQS is a Single protein structure of sequence from Chiba virus with HG, TLA and TAR as ligands. Full crystallographic information is available from OCA.

Reference

A norovirus protease structure provides insights into active and substrate binding site integrity., Nakamura K, Someya Y, Kumasaka T, Ueno G, Yamamoto M, Sato T, Takeda N, Miyamura T, Tanaka N, J Virol. 2005 Nov;79(21):13685-93. PMID:16227288

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