Phage major coat protein

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]

Phage coat Gp8
Single subunit of coat protein
Identifiers
SymbolPhage_Coat_Gp8
PfamPF05371
Pfam clanCL0371
InterProIPR008020
SCOP21fdm / SCOPe / SUPFAM
OPM superfamily67
OPM protein1ifk
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

References

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  1. ^ Marvin DA, Hale RD, Nave C, Helmer-Citterich M (January 1994). "Molecular models and structural comparisons of native and mutant class I filamentous bacteriophages Ff (fd, f1, M13), If1 and IKe" (PDF). J. Mol. Biol. 235 (1): 260–86. doi:10.1016/S0022-2836(05)80032-4. hdl:2108/15515. PMID 8289247.
This article incorporates text from the public domain Pfam and InterPro: IPR008020