7y96 | pdb_00007y96
Crystal structure of the carboxy-terminal domain of a coronavirus M protein fused with a split GFP
Structural highlights
FunctionVME1_BCHK5 Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins.[HAMAP-Rule:MF_04202][PROSITE-ProRule:PRU01275]GFP_AEQVI Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. Publication Abstract from PubMedThe 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. Crystal structure of the membrane (M) protein from a bat betacoronavirus.,Wang X, Yang Y, Sun Z, Zhou X PNAS Nexus. 2023 Jan 30;2(2):pgad021. doi: 10.1093/pnasnexus/pgad021. eCollection , 2023 Feb. PMID:36874273[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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