2c0x

MOLECULAR STRUCTURE OF FD FILAMENTOUS BACTERIOPHAGE REFINED WITH RESPECT TO X-RAY FIBRE DIFFRACTION AND SOLID-STATE NMR DATA

spinqualitylabelsall models 2c0x Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2c0x is a 1 chain structure with sequence from Enterobacteria phage fd. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solid-state NMR, 1 model Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CAPSD_BPFD Self assembles to form a helical capsid wrapping up the viral genomic DNA. The capsid displays a filamentous structure with a length of 760-1950 nm and a width of 6-8 nm. The virion assembly and budding take place at the host inner membrane (By similarity). Publication Abstract from PubMed Filamentous bacteriophage (Inovirus) is a simple and well-characterized model system. The phage particle, or virion, is about 60 angstroms in diameter and several thousand angstrom units long. The virions are assembled at the bacterial membrane as they extrude out of the host without killing it, an example of specific transport of nucleoprotein assemblages across membranes. The Ff group (fd, f1 and M13) has been especially widely studied. Models of virion assembly have been proposed based on a molecular model of the fd virion derived by X-ray fibre diffraction. A somewhat different model of the fd virion using solid-state NMR data has been proposed, not consistent with these models of assembly nor with the X-ray diffraction data. Here we show that reinterpreted NMR data are also consistent with the model derived from X-ray fibre diffraction studies, and discuss models of virion assembly. Molecular structure of fd (f1, M13) filamentous bacteriophage refined with respect to X-ray fibre diffraction and solid-state NMR data supports specific models of phage assembly at the bacterial membrane.,Marvin DA, Welsh LC, Symmons MF, Scott WR, Straus SK J Mol Biol. 2006 Jan 13;355(2):294-309. Epub 2005 Nov 8. PMID:16300790 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA