5wco

Matrix Protein (M1) of Infectious Salmon Anaemia Virus

spinqualitylabelsall models 5wco, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5wco is a 3 chain structure with sequence from Isav. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: NS2 (ISAV) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Many enveloped viruses encode a matrix protein. In the influenza A virus, the matrix protein M1 polymerizes into a rigid protein layer underneath the viral envelope to help enforce the shape and structural integrity of intact viruses. The influenza virus M1 is also known to mediate virus budding as well as the nuclear export of the viral nucleocapsids and their subsequent packaging into nascent viral particles. Despite extensive studies on the influenza A virus M1 (FLUA-M1), only crystal structures of its N-terminal domain are available. Here we report the crystal structure of the full-length M1 from another orthomyxovirus that infects fish, the infectious salmon anemia virus (ISAV). The structure of ISAV-M1 assumes the shape of an elbow, with its N domain closely resembling that of the FLUA-M1. The C domain, which is connected to the N domain through a flexible linker, is made of four alpha-helices packed as a tight bundle. In the crystal, ISAV-M1 monomers form infinite 2D arrays with a network of interactions involving both the N and C domains. Results from liposome flotation assays indicated that ISAV-M1 binds membrane via electrostatic interactions that are primarily mediated by a positively charged surface loop from the N domain. Cryoelectron tomography reconstruction of intact ISA virions identified a matrix protein layer adjacent to the inner leaflet of the viral membrane. The physical dimensions of the virion-associated matrix layer are consistent with the 2D ISAV-M1 crystal lattice, suggesting that the crystal lattice is a valid model for studying M1-M1, M1-membrane, and M1-RNP interactions in the virion. Crystal structure of an orthomyxovirus matrix protein reveals mechanisms for self-polymerization and membrane association.,Zhang W, Zheng W, Toh Y, Betancourt-Solis MA, Tu J, Fan Y, Vakharia VN, Liu J, McNew JA, Jin M, Tao YJ Proc Natl Acad Sci U S A. 2017 Aug 8;114(32):8550-8555. doi:, 10.1073/pnas.1701747114. Epub 2017 Jul 24. PMID:28739952 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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