 | This article relies largely or entirely on a
single source. (February 2015) |
| Phage coat Gp8 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Single subunit of coat protein | |||||||||
| Identifiers | |||||||||
| Symbol | Phage_Coat_Gp8 | ||||||||
| Pfam | PF05371 | ||||||||
| Pfam clan | CL0371 | ||||||||
| InterPro | IPR008020 | ||||||||
| SCOP2 | 1fdm / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 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]
References
- ^ 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 relies largely or entirely on a
single source. (February 2015) |
| Phage coat Gp8 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
|
Single subunit of coat protein | |||||||||
| Identifiers | |||||||||
| Symbol | Phage_Coat_Gp8 | ||||||||
| Pfam | PF05371 | ||||||||
| Pfam clan | CL0371 | ||||||||
| InterPro | IPR008020 | ||||||||
| SCOP2 | 1fdm / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 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]
References
- ^ 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.