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

Ting Xu1, Amy Ooi, Hooi Chen Lee

  • 1School of Biological Sciences, Nanyang Technological University, Singapore 637551, Singapore.

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
|March 3, 2006
PubMed

Insights

Crystallization of the SARS-CoV main proteinase (Mpro) provides a structural basis for developing inhibitors. This active enzyme crystal structure is key for designing drugs against SARS virus.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Virology

Background:

  • Severe acute respiratory syndrome coronavirus (SARS-CoV) relies on its main proteinase (Mpro) for viral polyprotein processing.
  • SARS-CoV Mpro is a critical target for developing antiviral inhibitors.

Purpose of the Study:

  • To obtain crystals of SARS-CoV Mpro suitable for structure-based drug design.
  • To characterize the Mpro crystal structure and assess its enzymatic activity.

Main Methods:

  • Crystallization of SARS-CoV Mpro at pH 6.5.
  • X-ray diffraction analysis to determine the crystal structure.
  • Assessment of catalytic site conformation for enzyme activity.

Main Results:

  • Orthorhombic crystals (space group P2(1)2(1)2) diffracting to 1.9 A resolution were obtained.
  • The biologically active dimer is formed through a crystallographic twofold axis.
  • The enzyme's catalytic site conformation indicates activity in the crystalline state.

Conclusions:

  • The determined crystal structure of SARS-CoV Mpro is suitable for structure-based inhibition studies.
  • This structural information facilitates the development of specific inhibitors against the SARS virus.

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