7Y96

Crystal structure of the carboxy-terminal domain of a coronavirus M protein fused with a split GFP

Summary for 7Y96

• Entry DOI: 10.2210/pdb7y96/pdb
• Related: 7Y9B
• Descriptor: Green fluorescent protein,Membrane protein (1 entity in total)
• Functional Keywords: m protein, cytosolic domain, sars-cov-2 related, membrane protein
• Biological source: Aequorea victoria; More
• Total number of polymer chains: 2
• Total formula weight: 76236.04

Authors

Wang, X.,Sun, Z.,Zhou, X. (deposition date: 2022-06-24, release date: 2022-08-17, Last modification date: 2024-11-06)

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

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: 36874273
DOI: 10.1093/pnasnexus/pgad021

Experimental method

X-RAY DIFFRACTION (3.415 Å)