The three-dimensional structure of bacteriophage PP7 from Pseudomonas aeruginosa at 3.7-A resolution.
The three-dimensional structure of phage PP7 from Pseudomonas aeruginosa has been determined to 3.7-A resolution. A comparison with distantly related small RNA phages showed that the biggest differences were found in the FG loops, forming the contacts around the fivefold and threefold axes. In contrast to the situation in other phages, the FG loops of phage PP7 are very similar in all three subunits. This supports the hypothesis that no switches are needed for the assembly control in these viruses. Some of the most conserved residues lie within the region involved in RNA binding in the related phages MS2 and seem to have the same function.
Tars
K
K
Department of Cell and Molecular Biology, Uppsala University, Uppsala, S-751 24, Sweden.
Fridborg
K
K
Bundule
M
M
Liljas
L
L
D000595:Amino Acid Sequence; D001665:Binding Sites; D002213:Capsid / Q000737:chemistry*; D003090:Coliphages / Q000737:chemistry; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017105:Pseudomonas Phages / Q000737:chemistry*; D011550:Pseudomonas aeruginosa / Q000821:virology*; D019065:Virus Assembly