7Y96 | pdb_00007y96

Crystal structure of the membrane (M) protein from a bat betacoronavirus.

(2023) PNAS Nexus 2: pgad021-pgad021

• PubMed: 36874273 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1093/pnasnexus/pgad021
• Primary Citation of Related Structures:  
  7Y96, 7Y9B


• 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 Pipistrellus 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.

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Organizational Affiliation: 
• State Key Laboratory of Biotherapy, Department of Integrated Traditional Chinese and Western Medicine, Rare Diseases Center, West China Hospital, Sichuan University, Chengdu, Sichuan 610041, China.