› 1fgp

Solution NMR

MEMBRANE PENETRATION DOMAIN OF THE MINOR COAT PROTEIN G3P OF PHAGE FD, NMR, 15 STRUCTURES

Released:
DOI: 10.2210/pdb1fgp/pdb
PDB entry 1fgp coloured by chain, ensemble of 15 models, front view.
PDB entry 1fgp coloured by chain, ensemble of 15 models, side view.
PDB entry 1fgp coloured by chain, ensemble of 15 models, top view.
Source organism: Enterobacteria phage fd
Primary publication:
A conserved infection pathway for filamentous bacteriophages is suggested by the structure of the membrane penetration domain of the minor coat protein g3p from phage fd.
Holliger P, Riechmann L
Structure 5 265-75 (1997)
PMID: 9032075

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137192 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Attachment protein G3P Chain: A
Molecule details ›
Chain: A
Length: 70 amino acids
Theoretical weight: 7.71 KDa
Source organism: Enterobacteria phage fd
Expression system: Escherichia coli
UniProt:
  • Canonical: P03661 (Residues: 20-85; Coverage: 16%)
Gene name: III
Sequence domains: Phage Coat Protein A
Structure domains: Phage FD Coat Protein,Membrane penetration domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Intrinsically disordered protein.
Dunker et al. (2001)
14 more

8 mentions without citation

Search for allosteric disulfide bonds in NMR structures.
Schmidt et al. (2007)
7 more