2BX3

Crystal Structure of SARS Coronavirus Main Proteinase (P43212)

Summary for 2BX3

• Entry DOI: 10.2210/pdb2bx3/pdb
• Related: 1O5S 1P4X 1P76 1P9S 1P9T 1P9U 1PA5 1PUK 1Q1X 1Q2W 1Q4Z 1QZ8 1SSK 1SXF 1UJ1 1UK2 1UK3 1UK4 1UW7 1WNC 1XAK 1XJP 1XJR 2BW6 2BX4
• Descriptor: 3C-like proteinase nsp5 (2 entities in total)
• Functional Keywords: sars, hydrolase, anti-parallel b-barrel, anti-parallel a- helices, viral protein
• Biological source: SARS coronavirus Sin2774
• Total number of polymer chains: 1
• Total formula weight: 33876.64

Authors

Verschueren, K.H.G.,Mesters, J.R.,Hilgenfeld, R. (deposition date: 2005-07-22, release date: 2005-09-26, Last modification date: 2024-01-31)

Primary citation

Tan, J.,Verschueren, K.H.G.,Anand, K.,Shen, J.,Yang, M.,Xu, Y.,Rao, Z.,Bigalke, J.,Heisen, B.,Mesters, J.R.,Chen, K.,Shen, X.,Jiang, H.,Hilgenfeld, R.
Ph-Dependent Conformational Flexibility of the Sars-Cov Main Proteinase (M(Pro)) Dimer: Molecular Dynamics Simulations and Multiple X-Ray Structure Analyses.
J.Mol.Biol., 354:25-, 2005

PubMed Abstract: The SARS coronavirus main proteinase (M(pro)) is a key enzyme in the processing of the viral polyproteins and thus an attractive target for the discovery of drugs directed against SARS. The enzyme has been shown by X-ray crystallography to undergo significant pH-dependent conformational changes. Here, we assess the conformational flexibility of the M(pro) by analysis of multiple crystal structures (including two new crystal forms) and by molecular dynamics (MD) calculations. The MD simulations take into account the different protonation states of two histidine residues in the substrate-binding site and explain the pH-activity profile of the enzyme. The low enzymatic activity of the M(pro) monomer and the need for dimerization are also discussed.

PubMed: 16242152
DOI: 10.1016/J.JMB.2005.09.012

Experimental method

X-RAY DIFFRACTION (2 Å)