|Entry||Database: PDB / ID: 1fgp|
|Title||MEMBRANE PENETRATION DOMAIN OF THE MINOR COAT PROTEIN G3P OF PHAGE FD, NMR, 15 STRUCTURES|
|Components||FD GENE 3 PROTEIN|
|Keywords||VIRAL PROTEIN / PHAGE COAT PROTEIN / SH3 DOMAIN / PH DOMAIN / PDZ DOMAIN / FD PHAGE / FILAMENTOUS PAHGE / PHAGE INFECTION / PTB DOMAIN|
|Function / homology|
Function and homology information
viral entry into host cell via pilus basal pore / viral extrusion / virion attachment to host cell pilus / adhesion receptor-mediated virion attachment to host cell / entry receptor-mediated virion attachment to host cell / host cell membrane / viral capsid / integral component of membrane
Similarity search - Function
Bacteriophage, G3P, N2-domain superfamily / Phage FD Coat Protein, Membrane penetration domain / Phage FD Coat Protein,Membrane penetration domain / Phage Coat Protein A / Attachment protein G3P, N-terminal / Attachment protein G3P, N-terminal domain superfamily / Roll / Mainly Beta
Similarity search - Domain/homology
Attachment protein G3P
Similarity search - Component
|Biological species||Enterobacteria phage fd (virus)|
|Method||SOLUTION NMR / simulated annealing|
|Authors||Holliger, P. / Riechmann, L.|
|Citation||Journal: Structure / Year: 1997|
Title: 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.
Authors: Holliger, P. / Riechmann, L.
|Structure viewer||Molecule: |
Downloads & links
A: FD GENE 3 PROTEIN
|#1: Protein|| |
Mass: 7711.479 Da / Num. of mol.: 1 / Fragment: DOMAIN 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Enterobacteria phage fd (virus) / Genus: InovirusFf phages / Species: Enterobacteria phage M13 / Plasmid: PUC119 / Cellular location (production host): SUPERNATANT / Production host: Escherichia coli (E. coli) / References: UniProt: P03661
|Experiment||Method: SOLUTION NMR|
|NMR experiment||Type: 15N + 13C NOESY-HMQC|
|Sample conditions||pH: 6.2 / Temperature: 303 K|
*PLUSMethod: other / Details: NMR
|NMR spectrometer||Type: Bruker AMX500 / Manufacturer: Bruker / Model: AMX500 / Field strength: 500 MHz|
|Refinement||Method: simulated annealing / Software ordinal: 1 / Details: SEE JRNL REFERENCE.|
|NMR ensemble||Conformer selection criteria: LOWEST TOTAL ENERGIES / Conformers calculated total number: 50 / Conformers submitted total number: 15|
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