1jmu

Crystal Structure of the Reovirus mu1/sigma3 Complex

spinqualitylabelsall models 1jmu, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1jmu is a 9 chain structure with sequence from Reovirus sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: ACE, BOG, CL, SO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MU1_REOVL Major outer capsid protein involved in host cell membrane penetration. In the endocytic compartment, outer-capsid protein sigma-3 is removed by cathepsin proteases, which exposes the viral membrane-penetration protein mu-1. Both myristoylated peptides mu-1N and phi are released during infectious subvirion particles (ISVP) formation in the endosome. They associate with host membranes and mu-1N induces permeabilization and delivery of transcriptionally active viral particles into the host cell cytoplasm. Seems to induce apoptosis in the host cell. The viral outer shell polypeptides, of which mu-1 is one, impose structural constraints that prevent elongation of nascent transcripts by the RNA-dependent RNA polymerase lambda-3. 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 Cell entry by nonenveloped animal viruses requires membrane penetration without membrane fusion. The reovirus penetration agent is the outer-capsid protein, Mu1. The structure of Mu1, complexed with its "protector" protein, Sigma3, and the fit of this Mu1(3)Sigma3(3) heterohexameric complex into the cryoEM image of an intact virion, reveal molecular events essential for viral penetration. Autolytic cleavage divides Mu1 into myristoylated Mu1N and Mu1C. A long hydrophobic pocket can receive the myristoyl group. Dissociation of Mu1N, linked to a major conformational change of the entire Mu1 trimer, must precede myristoyl-group insertion into the cellular membrane. A myristoyl switch, coupling exposure of the fatty acid chain, autolytic cleavage of Mu1N, and long-range molecular rearrangement of Mu1C, thus appears to be part of the penetration mechanism. Structure of the reovirus membrane-penetration protein, Mu1, in a complex with is protector protein, Sigma3.,Liemann S, Chandran K, Baker TS, Nibert ML, Harrison SC Cell. 2002 Jan 25;108(2):283-95. PMID:11832217 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Virus coat proteins 3D structures

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