6W02
Crystal Structure of ADP ribose phosphatase of NSP3 from SARS CoV-2 in the complex with ADP ribose
Summary for 6W02
| Entry DOI | 10.2210/pdb6w02/pdb |
| Related | 6VXS |
| Descriptor | Non-structural protein 3, ADENOSINE-5-DIPHOSPHORIBOSE, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | sars corona virus, macro domain, adp-ribose, structural genomics, center for structural genomics of infectious diseases, csgid, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) |
| Total number of polymer chains | 2 |
| Total formula weight | 37732.24 |
| Authors | Michalska, K.,Kim, Y.,Jedrzejczak, R.,Maltseva, N.,Endres, M.,Mesecar, A.,Joachimiak, A.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2020-02-28, release date: 2020-03-11, Last modification date: 2023-10-11) |
| Primary citation | Michalska, K.,Kim, Y.,Jedrzejczak, R.,Maltseva, N.I.,Stols, L.,Endres, M.,Joachimiak, A. Crystal structures of SARS-CoV-2 ADP-ribose phosphatase: from the apo form to ligand complexes. Iucrj, 7:814-824, 2020 Cited by PubMed Abstract: Among 15 nonstructural proteins (Nsps), the newly emerging Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) encodes a large, multidomain Nsp3. One of its units is the ADP-ribose phosphatase domain (ADRP; also known as the macrodomain, MacroD), which is believed to interfere with the host immune response. Such a function appears to be linked to the ability of the protein to remove ADP-ribose from ADP-ribosylated proteins and RNA, yet the precise role and molecular targets of the enzyme remain unknown. Here, five high-resolution (1.07-2.01 Å) crystal structures corresponding to the apo form of the protein and its complexes with 2-(-morpholino)ethanesulfonic acid (MES), AMP and ADP-ribose have been determined. The protein is shown to undergo conformational changes to adapt to the ligand in the manner previously observed in close homologues from other viruses. A conserved water molecule is also identified that may participate in hydrolysis. This work builds foundations for future structure-based research on ADRP, including the search for potential antiviral therapeutics. PubMed: 32939273DOI: 10.1107/S2052252520009653 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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