Structure of the SARS coronavirus main proteinase as an active C2 crystallographic dimer

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Ting XuJulien Lescar

Abstract

The 34 kDa main proteinase (Mpro) 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 Mpro 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(1)2(1)2 that diffract to a resolution of 1.9 A. 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.

References

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Citations

Feb 22, 2012·Biotechnology Letters·Thi Thanh Hanh NguyenDoman Kim
May 3, 2011·Protein & Cell·Bin Xia, Xue Kang
May 25, 2011·Journal of Chemical Information and Modeling·Prasenjit MukherjeeMitchell Avery
Feb 1, 2012·Biomolecular Concepts·Yuichi Someya
Nov 7, 2006·Current Opinion in Structural Biology·Jeroen R MestersRolf Hilgenfeld
May 14, 2016·Scientific Reports·Sarah E St JohnAndrew D Mesecar
Mar 28, 2006·The Journal of Biological Chemistry·Hao ChenLuhua Lai
Jun 15, 2021·Journal of Chemical Information and Modeling·Eunice ChoShozeb Haider
Aug 24, 2021·Journal of Biomolecular Structure & Dynamics·Suvankar GhoshKrishna Pada Bhabak

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Methods Mentioned

BETA
PCR

Software Mentioned

REFMAC
CCP
AMoRe
ARP
wARP
PROCHECK

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