7C33

Macro domain of SARS-CoV-2 in complex with ADP-ribose

Summary for 7C33

• Entry DOI: 10.2210/pdb7c33/pdb
• Descriptor: Non-structural protein 3, ADENOSINE-5-DIPHOSPHORIBOSE (2 entities in total)
• Functional Keywords: covid-19, sars-cov-2, macro domain, adp-ribose, hydrolase
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV)
• Total number of polymer chains: 4
• Total formula weight: 77639.39

Authors

Lin, M.H.,Hsu, C.H. (deposition date: 2020-05-11, release date: 2020-11-11, Last modification date: 2023-11-29)

Primary citation

Lin, M.H.,Chang, S.C.,Chiu, Y.C.,Jiang, B.C.,Wu, T.H.,Hsu, C.H.
Structural, Biophysical, and Biochemical Elucidation of the SARS-CoV-2 Nonstructural Protein 3 Macro Domain.
Acs Infect Dis., 6:2970-2978, 2020

PubMed Abstract: The pandemic outbreak of a novel coronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has threatened the global public health and economy since late December 2019. SARS-CoV-2 encodes the conserved macro domain within nonstructural protein 3, which may reverse cellular ADP-ribosylation and potentially cut the signal of a viral infection in the cell. Herein, we report that the SARS-CoV-2 macro domain was examined as a poly-ADP-ribose (ADPR) binding module and possessed mono-ADPR cleavage enzyme activity. After confirming the ADPR binding ability via a biophysical approach, the X-ray crystal structure of the SARS-CoV-2 macro domain was determined and structurally compared with those of other viruses. This study provides structural, biophysical, and biochemical bases to further evaluate the role of the SARS-CoV-2 macro domain in the host response via ADP-ribose binding but also as a potential target for drug design against COVID-19.

PubMed: 32946224
DOI: 10.1021/acsinfecdis.0c00441

Experimental method

X-RAY DIFFRACTION (3.83 Å)