7Y9B
Crystal structure of the membrane (M) protein of a SARS-COV-2-related coronavirus
Summary for 7Y9B
Entry DOI | 10.2210/pdb7y9b/pdb |
Related | 7Y96 |
Descriptor | Membrane protein, 3,6,9,12,15-PENTAOXATRICOSAN-1-OL (3 entities in total) |
Functional Keywords | m protein, sars-cov-2 related, membrane protein |
Biological source | Pipistrellus bat coronavirus HKU5 |
Total number of polymer chains | 4 |
Total formula weight | 100321.84 |
Authors | |
Primary citation | Wang, X.,Yang, Y.,Sun, Z.,Zhou, X. Crystal structure of the membrane (M) protein from a bat betacoronavirus. Pnas Nexus, 2:pgad021-pgad021, 2023 Cited by PubMed Abstract: The membrane (M) protein is the most abundant structural protein of coronaviruses including MERS-CoV, SARS-CoV, and SARS-CoV-2, and plays a central role in virus assembly through its interaction with various partner proteins. However, mechanistic details about how M protein interacts with others remain elusive due to lack of high-resolution structures. Here, we present the first crystal structure of a betacoronavirus M protein from bat coronavirus HKU5 (batCOV5-M), which is closely related to MERS-CoV, SARS-CoV, and SARS-CoV-2 M proteins. Furthermore, an interaction analysis indicates that the carboxy-terminus of the batCOV5 nucleocapsid (N) protein mediates its interaction with batCOV5-M. Combined with a computational docking analysis an M-N interaction model is proposed, providing insight into the mechanism of M protein-mediated protein interactions. PubMed: 36874273DOI: 10.1093/pnasnexus/pgad021 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.214 Å) |
Structure validation
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