Phage major coat protein explained

Symbol:Phage_Coat_Gp8
Phage coat Gp8
Pfam:PF05371
Pfam Clan:CL0371
Interpro:IPR008020
Scop:1fdm
Opm Family:67
Opm Protein:1ifk

In molecular biology, a phage major coat protein is an alpha-helical protein that forms a viral envelope of filamentous bacteriophages. These bacteriophages are flexible rods, about one to two micrometres long and six nm in diameter, with a helical shell of protein subunits surrounding a DNA core. The approximately 50-residue subunit of the major coat protein is largely alpha-helix, and the axis of the alpha-helix makes a small angle with the axis of the virion. The protein shell can be considered in three sections: the outer surface, occupied by the N-terminal region of the subunit and rich in acidic residues that give the virion a low isoelectric point; the interior of the shell (including a 19-residue stretch of apolar side-chains) where protein subunits interact, mainly with each other; and the inner surface (occupied by the C-terminal region of the subunit), rich in positively charged residues that interact with the DNA core.[1]

Notes and References

  1. Marvin DA, Hale RD, Nave C, Helmer-Citterich M . Molecular models and structural comparisons of native and mutant class I filamentous bacteriophages Ff (fd, f1, M13), If1 and IKe . J. Mol. Biol. . 235 . 1 . 260–86 . January 1994 . 8289247 . 10.1016/S0022-2836(05)80032-4. 2108/15515 .