1fpv

STRUCTURE DETERMINATION OF FELINE PANLEUKOPENIA VIRUS EMPTY PARTICLES

spinqualitylabelsall models 1fpv, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1fpv is a 1 chain structure with sequence from Fplv. The May 2010 RCSB PDB Molecule of the Month feature on Parvoviruses by David Goodsell is 10.2210/rcsb_pdb/mom_2010_5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CAPSD_FPV19] Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Capsid proteins are responsible for the attachment to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and putative nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus (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 Various crystal forms of the single-stranded DNA, feline panleukopenia virus (FPV), a parvovirus, have been grown of both full virions and empty particles. The structure of empty particles crystallized in an orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions a = 380.1 A, b = 379.3 A, and c = 350.9 A, has been determined to 3.3 A resolution. The data were collected using oscillation photography with synchrotron radiation. The orientations of the empty capsids in the unit cell were determined using a self-rotation function and their positions were obtained with an R-factor search using canine parvovirus (CPV) as a model. Phases were then calculated, based on the CPV model, to 6.0 A resolution and gradually extended to 3.3 A resolution by molecular replacement electron density averaging. The resultant electron density was readily interpreted in terms of the known amino acid sequence. The structure is contrasted to that of CPV in terms of host range, neutralization by antibodies, hemagglutination properties, and binding of genomic DNA. Structure determination of feline panleukopenia virus empty particles.,Agbandje M, McKenna R, Rossmann MG, Strassheim ML, Parrish CR Proteins. 1993 Jun;16(2):155-71. PMID:8392729 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Virus coat protein

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