4n23

Crystal structure of the GP2 Core Domain from the California Academy of Science Virus, monoclinic symmetry

spinqualitylabelsall models 4n23, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4n23 is a 3 chain structure with sequence from CAS virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: MPD, MRD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function J7H5L9_9VIRU Publication Abstract from PubMed Fusion of the viral and host cell membranes is a necessary first step for infection by enveloped viruses and is mediated by the envelope glycoprotein. The transmembrane subunits from the structurally defined "class I" glycoproteins adopt an alpha-helical "trimer-of-hairpins" conformation during the fusion pathway. Here, we present our studies on the envelope glycoprotein transmembrane subunit, GP2, of the CAS virus (CASV). CASV was recently identified from annulated tree boas (Corallus annulatus) with inclusion body disease and is implicated in the disease etiology. We have generated and characterized two protein constructs consisting of the predicted CASV GP2 core domain. The crystal structure of the CASV GP2 post-fusion conformation indicates a trimeric alpha-helical bundle that is highly similar to those of Ebola virus and Marburg virus GP2 despite CASV genome homology to arenaviruses. Denaturation studies demonstrate that the stability of CASV GP2 is pH dependent with higher stability at lower pH; we propose that this behavior is due to a network of interactions among acidic residues that would destabilize the alpha-helical bundle under conditions where the side chains are deprotonated. The pH-dependent stability of the post-fusion structure has been observed in Ebola virus and Marburg virus GP2, as well as other viruses that enter via the endosome. Infection experiments with CASV and the related Golden Gate virus support a mechanism of entry that requires endosomal acidification. Our results suggest that, despite being primarily arenavirus like, the transmembrane subunit of CASV is extremely similar to the filoviruses. Structural Characterization of the Glycoprotein GP2 Core Domain from the CAS Virus, a Novel Arenavirus-Like Species.,Koellhoffer JF, Dai Z, Malashkevich VN, Stenglein MD, Liu Y, Toro R, Harrison J, Chandran K, Derisi JL, Almo SC, Lai JR J Mol Biol. 2013 Dec 12. pii: S0022-2836(13)00751-1. doi:, 10.1016/j.jmb.2013.12.009. PMID:24333483 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glycoprotein GP 3D structures

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