9L9T

Crystal structure of a coronaviral M protein in complex with a C-terminal peptide of the N protein

Summary for 9L9T

• Entry DOI: 10.2210/pdb9l9t/pdb
• Descriptor: Membrane protein, N protein peptide poly-Ala model, 3,6,9,12,15-PENTAOXATRICOSAN-1-OL, ... (4 entities in total)
• Functional Keywords: m protein, n protein, interaction, coronavirus, membrane protein
• Biological source: Pipistrellus bat coronavirus HKU5; More
• Total number of polymer chains: 4
• Total formula weight: 50907.73

Authors

Wang, X.,Sun, Z.,Zhou, X. (deposition date: 2024-12-31, release date: 2025-11-05)

Primary citation

Wang, X.,Yang, S.,Yang, P.,Sun, Z.,Zhou, X.
Binding of an N protein peptide to M protein of a bat coronavirus.
J.Struct.Biol., 217:108234-108234, 2025

PubMed Abstract: The interaction between the membrane (M) protein and the nucleocapsid (N) protein of coronaviruses plays a crucial role in virus assembly and morphogenesis. Previous studies indicate that one M-N interaction occurs between M protein and the carboxy-terminus of N protein. However, the mechanistic details of M-N interactions remain unclear. Here, we present a complex structure of an N protein carboxy-terminal peptide bound to M protein from Pipistrellus bat coronavirus HKU5. The structure shows that the M-N peptide binding site includes a "horizontal" groove located between the carboxy-terminal domain and the transmembrane domain of M protein. Combined with molecular docking and binding analysis, our results provide structural insight into the binding mechanism between M and N proteins of a coronavirus.

PubMed: 40664277
DOI: 10.1016/j.jsb.2025.108234

Experimental method

X-RAY DIFFRACTION (3.142 Å)