2w2r

Structure of the vesicular stomatitis virus matrix protein

spinqualitylabelsall models 2w2r, resolution 1.83Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2w2r is a 1 chain structure with sequence from Vesicular stomatitis virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.83Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MATRX_VSNJO Plays a major role in assembly and budding of virion. Condensates the ribonucleocapsid core during virus assembly. Shut off cellular transcription by inhibiting mRNA nuclear export through direct interaction with host RAE1-NUP98 complex. This shutoff presumably inhibits interferon signaling and thus establishment of antiviral state in virus infected cells. Induces cell-rounding, cytoskeleton disorganization and apoptosis in infected cell (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The matrix (M) proteins of rhabdoviruses are multifunctional proteins essential for virus maturation and budding that also regulate the expression of viral and host proteins. We have solved the structures of M from the vesicular stomatitis virus serotype New Jersey (genus: Vesiculovirus) and from Lagos bat virus (genus: Lyssavirus), revealing that both share a common fold despite sharing no identifiable sequence homology. Strikingly, in both structures a stretch of residues from the otherwise-disordered N terminus of a crystallographically adjacent molecule is observed binding to a hydrophobic cavity on the surface of the protein, thereby forming non-covalent linear polymers of M in the crystals. While the overall topology of the interaction is conserved between the two structures, the molecular details of the interactions are completely different. The observed interactions provide a compelling model for the flexible self-assembly of the matrix protein during virion morphogenesis and may also modulate interactions with host proteins. Rhabdovirus matrix protein structures reveal a novel mode of self-association.,Graham SC, Assenberg R, Delmas O, Verma A, Gholami A, Talbi C, Owens RJ, Stuart DI, Grimes JM, Bourhy H PLoS Pathog. 2008 Dec;4(12):e1000251. Epub 2008 Dec 26. PMID:19112510 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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