4v5t

X-ray structure of the Grapevine Fanleaf virusX-ray structure of the Grapevine Fanleaf virus

Structural highlights 4v5t is a 60 chain structure with sequence from Grapevine fanleaf virus. This structure supersedes the now removed PDB entries 2y7t, 2y7u and 2y7v. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function POL2_GFLV Protein 2A: implicated in RNA2 replication. Could also be required for nematode transmission of the virus. Movement protein: transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Acts by forming a tubular structure at the host plasmodesmata, enlarging it enough to allow free passage of virion capsids. Publication Abstract from PubMed Many animal and plant viruses rely on vectors for their transmission from host to host. Grapevine fanleaf virus (GFLV), a picorna-like virus from plants, is transmitted specifically by the ectoparasitic nematode Xiphinema index. The icosahedral capsid of GFLV, which consists of 60 identical coat protein subunits (CP), carries the determinants of this specificity. Here, we provide novel insight into GFLV transmission by nematodes through a comparative structural and functional analysis of two GFLV variants. We isolated a mutant GFLV strain (GFLV-TD) poorly transmissible by nematodes, and showed that the transmission defect is due to a glycine to aspartate mutation at position 297 (Gly297Asp) in the CP. We next determined the crystal structures of the wild-type GFLV strain F13 at 3.0 A and of GFLV-TD at 2.7 A resolution. The Gly297Asp mutation mapped to an exposed loop at the outer surface of the capsid and did not affect the conformation of the assembled capsid, nor of individual CP molecules. The loop is part of a positively charged pocket that includes a previously identified determinant of transmission. We propose that this pocket is a ligand-binding site with essential function in GFLV transmission by X. index. Our data suggest that perturbation of the electrostatic landscape of this pocket affects the interaction of the virion with specific receptors of the nematode's feeding apparatus, and thereby severely diminishes its transmission efficiency. These data provide a first structural insight into the interactions between a plant virus and a nematode vector. Structural Insights into Viral Determinants of Nematode Mediated Grapevine fanleaf virus Transmission.,Schellenberger P, Sauter C, Lorber B, Bron P, Trapani S, Bergdoll M, Marmonier A, Schmitt-Keichinger C, Lemaire O, Demangeat G, Ritzenthaler C PLoS Pathog. 2011 May;7(5):e1002034. Epub 2011 May 19. PMID:21625570 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Virus coat proteins 3D structures

spinqualitylabelsall models 4v5t, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image