5DUS
Crystal structure of MERS-CoV macro domain in complex with ADP-ribose
Summary for 5DUS
| Entry DOI | 10.2210/pdb5dus/pdb |
| Descriptor | ORF1a, ADENOSINE-5-DIPHOSPHORIBOSE, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | ligand, complex, macro domain, adp-ribose, viral protein |
| Biological source | Middle East respiratory syndrome coronavirus |
| Cellular location | Host membrane ; Multi-pass membrane protein : T2B9G2 |
| Total number of polymer chains | 1 |
| Total formula weight | 18805.28 |
| Authors | Cho, C.-C.,Lin, M.-H.,Chuang, C.-Y.,Hsu, C.-H. (deposition date: 2015-09-20, release date: 2016-01-13, Last modification date: 2024-03-20) |
| Primary citation | Cho, C.-C.,Lin, M.-H.,Chuang, C.-Y.,Hsu, C.-H. Macro Domain from Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Is an Efficient ADP-ribose Binding Module: CRYSTAL STRUCTURE AND BIOCHEMICAL STUDIES J.Biol.Chem., 291:4894-4902, 2016 Cited by PubMed Abstract: The newly emerging Middle East respiratory syndrome coronavirus (MERS-CoV) encodes the conserved macro domain within non-structural protein 3. However, the precise biochemical function and structure of the macro domain is unclear. Using differential scanning fluorimetry and isothermal titration calorimetry, we characterized the MERS-CoV macro domain as a more efficient adenosine diphosphate (ADP)-ribose binding module than macro domains from other CoVs. Furthermore, the crystal structure of the MERS-CoV macro domain was determined at 1.43-Å resolution in complex with ADP-ribose. Comparison of macro domains from MERS-CoV and other human CoVs revealed structural differences in the α1 helix alters how the conserved Asp-20 interacts with ADP-ribose and may explain the efficient binding of the MERS-CoV macro domain to ADP-ribose. This study provides structural and biophysical bases to further evaluate the role of the MERS-CoV macro domain in the host response via ADP-ribose binding but also as a potential target for drug design. PubMed: 26740631DOI: 10.1074/jbc.M115.700542 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.432 Å) |
Structure validation
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