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Title: Structure of the SARS coronavirus main proteinase as an active C{sub 2} crystallographic dimer

Abstract

An orthorhombic crystal form of the SARS CoV main proteinase diffracting to a resolution of 1.9 Å is reported. The conformation of residues in the catalytic site indicates an active enzyme. The 34 kDa main proteinase (M{sup pro}) from the severe acute respiratory syndrome coronavirus (SARS-CoV) plays an important role in the virus life cycle through the specific processing of viral polyproteins. As such, SARS-CoV M{sup pro} is a key target for the identification of specific inhibitors directed against the SARS virus. With a view to facilitating the development of such compounds, crystals were obtained of the enzyme at pH 6.5 in the orthorhombic space group P2{sub 1}2{sub 1}2 that diffract to a resolution of 1.9 Å. These crystals contain one monomer per asymmetric unit and the biologically active dimer is generated via the crystallographic twofold axis. The conformation of the catalytic site indicates that the enzyme is active in the crystalline form and thus suitable for structure-based inhibition studies.

Authors:
; ; ;  [1];  [2];  [1]
  1. School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551 (Singapore)
  2. Institute of Molecular and Cell Biology (Singapore)
Publication Date:
OSTI Identifier:
22356178
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 61; Journal Issue: Pt 11; Other Information: PMCID: PMC1978130; PMID: 16511208; PUBLISHER-ID: sw5004; OAI: oai:pubmedcentral.nih.gov:1978130; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALS; DIMERS; MONOMERS; PROCESSING; RESOLUTION; SPACE GROUPS

Citation Formats

Xu, Ting, Ooi, Amy, Lee, Hooi Chen, Wilmouth, Rupert, Liu, Ding Xiang, and Lescar, Julien, E-mail: julien@ntu.edu.sg. Structure of the SARS coronavirus main proteinase as an active C{sub 2} crystallographic dimer. United Kingdom: N. p., 2005. Web. doi:10.1107/S1744309105033257.
Xu, Ting, Ooi, Amy, Lee, Hooi Chen, Wilmouth, Rupert, Liu, Ding Xiang, & Lescar, Julien, E-mail: julien@ntu.edu.sg. Structure of the SARS coronavirus main proteinase as an active C{sub 2} crystallographic dimer. United Kingdom. doi:10.1107/S1744309105033257.
Xu, Ting, Ooi, Amy, Lee, Hooi Chen, Wilmouth, Rupert, Liu, Ding Xiang, and Lescar, Julien, E-mail: julien@ntu.edu.sg. Tue . "Structure of the SARS coronavirus main proteinase as an active C{sub 2} crystallographic dimer". United Kingdom. doi:10.1107/S1744309105033257.
@article{osti_22356178,
title = {Structure of the SARS coronavirus main proteinase as an active C{sub 2} crystallographic dimer},
author = {Xu, Ting and Ooi, Amy and Lee, Hooi Chen and Wilmouth, Rupert and Liu, Ding Xiang and Lescar, Julien, E-mail: julien@ntu.edu.sg},
abstractNote = {An orthorhombic crystal form of the SARS CoV main proteinase diffracting to a resolution of 1.9 Å is reported. The conformation of residues in the catalytic site indicates an active enzyme. The 34 kDa main proteinase (M{sup pro}) from the severe acute respiratory syndrome coronavirus (SARS-CoV) plays an important role in the virus life cycle through the specific processing of viral polyproteins. As such, SARS-CoV M{sup pro} is a key target for the identification of specific inhibitors directed against the SARS virus. With a view to facilitating the development of such compounds, crystals were obtained of the enzyme at pH 6.5 in the orthorhombic space group P2{sub 1}2{sub 1}2 that diffract to a resolution of 1.9 Å. These crystals contain one monomer per asymmetric unit and the biologically active dimer is generated via the crystallographic twofold axis. The conformation of the catalytic site indicates that the enzyme is active in the crystalline form and thus suitable for structure-based inhibition studies.},
doi = {10.1107/S1744309105033257},
journal = {Acta Crystallographica. Section F},
number = Pt 11,
volume = 61,
place = {United Kingdom},
year = {Tue Nov 01 00:00:00 EST 2005},
month = {Tue Nov 01 00:00:00 EST 2005}
}