1HGV

Filamentous Bacteriophage PH75

Summary for 1HGV

• Entry DOI: 10.2210/pdb1hgv/pdb
• Related: 1HGZ 1HH0 1IFN 1IFP 1PFI 1QL1 1QL2 2IFM 2IFN 3IFM 4IFM
• Descriptor: PH75 INOVIRUS MAJOR COAT PROTEIN (1 entity in total)
• Functional Keywords: virus, virus coat protein, helical virus coat protein, ssdna viruses, inovirus, filamentous bacteriophage, thermophiles, membrane proteins, icosahedral virus
• Biological source: BACTERIOPHAGE PH75 (INOVIRUS PH75)
• Cellular location: Virion (Potential): P82889
• Total number of polymer chains: 1
• Total formula weight: 4816.58

Authors

Pederson, D.M.,Welsh, L.C.,Marvin, D.A.,Sampson, M.,Perham, R.N.,Yu, M.,Slater, M.R. (deposition date: 2000-12-15, release date: 2001-06-01, Last modification date: 2023-12-13)

Primary citation

Pederson, D.M.,Welsh, L.C.,Marvin, D.A.,Sampson, M.,Perham, R.N.,Yu, M.,Slater, M.R.
The Protein Capsid of Filamentous Bacteriophage Ph75 from Thermus Thermophilus
J.Mol.Biol., 309:401-, 2001

PubMed Abstract: The PH75 strain of filamentous bacteriophage (Inovirus) grows in the thermophilic bacterium Thermus thermophilus at 70 degrees C. We have characterized the viral DNA and determined the amino acid sequence of the major coat protein, p8. The p8 protein is synthesized without a leader sequence, like that of bacteriophage Pf3 but unlike that of bacteriophage Pf1, both of which grow in the mesophile Pseudomonas aeruginosa. X-ray diffraction patterns from ordered fibres of the PH75 virion are similar to those from bacteriophages Pf1 and Pf3, indicating that the protein capsid of the PH75 virion has the same helix symmetry and subunit shape, even though the primary structures of the major coat proteins are quite different and the virions assemble at very different temperatures. We have used this information to build a molecular model of the PH75 protein capsid based on that of Pf1, and refined the model by simulated annealing, using fibre diffraction data extending to 2.4 A resolution in the meridional direction and to 3.1 A resolution in the equatorial direction. The common design may reflect a fundamental motif of alpha-helix packing, although differences exist in the DNA packaging and in the means of insertion of the major coat protein of these filamentous bacteriophages into the membrane of the host bacterial cell. These may reflect differences in the assembly mechanisms of the virions.

PubMed: 11371161
DOI: 10.1006/JMBI.2001.4685

Experimental method

FIBER DIFFRACTION (2.4 Å)