2C0W

Molecular Structure of fd Filamentous Bacteriophage Refined with Respect to X-ray Fibre Diffraction

Summary for 2C0W

• Entry DOI: 10.2210/pdb2c0w/pdb
• Related: 2C0X
• Descriptor: COAT PROTEIN B (1 entity in total)
• Functional Keywords: virus, capsid protein, filamentous bacteriophage, membrane protein, structural protein, helical virus
• Biological source: ENTEROBACTERIA PHAGE FD
• Cellular location: Virion (Potential): P69539
• Total number of polymer chains: 1
• Total formula weight: 5212.02

Authors

Marvin, D.A.,Welsh, L.C.,Symmons, M.F.,Scott, W.R.P.,Straus, S.K. (deposition date: 2005-09-08, release date: 2005-12-14, Last modification date: 2024-02-14)

Primary citation

Marvin, D.A.,Welsh, L.C.,Symmons, M.F.,Scott, W.R.P.,Straus, S.K.
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.
J.Mol.Biol., 355:294-, 2006

PubMed Abstract: 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.

PubMed: 16300790
DOI: 10.1016/J.JMB.2005.10.048

Experimental method

FIBER DIFFRACTION (3.2 Å)