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

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.

SUBMITTER: Xu T

PROVIDER: S-EPMC1978130 | biostudies-literature | 2005 Nov

REPOSITORIES: biostudies-literature

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

Xu Ting T Ooi Amy A Lee Hooi Chen HC Wilmouth Rupert R Liu Ding Xiang DX Lescar Julien J

Acta crystallographica. Section F, Structural biology and crystallization communications 20051020 Pt 11

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 resolut ...[more]

PMID: 16511208

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