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7Y9B

Crystal structure of the membrane (M) protein of a SARS-COV-2-related coronavirus

Summary for 7Y9B
Entry DOI10.2210/pdb7y9b/pdb
Related7Y96
DescriptorMembrane protein, 3,6,9,12,15-PENTAOXATRICOSAN-1-OL (3 entities in total)
Functional Keywordsm protein, sars-cov-2 related, membrane protein
Biological sourcePipistrellus bat coronavirus HKU5
Total number of polymer chains4
Total formula weight100321.84
Authors
Wang, X.,Sun, Z.,Zhou, X. (deposition date: 2022-06-24, release date: 2022-08-17, Last modification date: 2023-11-29)
Primary citationWang, 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: 36874273
DOI: 10.1093/pnasnexus/pgad021
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.214 Å)
Structure validation

237735

数据于2025-06-18公开中

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