DP00034: Attachment protein G3PFASTA viewXML view

General information
DisProt:DP00034
Name:Attachment protein G3P
Synonym(s):G3P_BPFD
Gene 3 protein
G3P
Minor phage coat protein G3P
First appeared in release:Release 1.0 (08/01/2003)
UniProt:P03661
UniGene: 
SwissProt: G3P_BPFD
TrEMBL:  
NCBI (GI): 116658
Source organism:Enterobacteria phage fd (Bacteriophage fd)
Sequence length:424
Percent disordered:6%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MKKLLFAIPL VVPFYSHSAE TVESCLAKPH TENSFTNVWK DDKTLDRYAN YEGCLWNATG - 60
VVVCTGDETQ CYGTWVPIGL AIPENEGGGS EGGGSEGGGS EGGGTKPPEY GDTPIPGYTY - 120
INPLDGTYPP GTEQNPANPN PSLEESQPLN TFMFQNNRFR NRQGALTVYT GTVTQGTDPV - 180
KTYYQYTPVS SKAMYDAYWN GKFRDCAFHS GFNEDPFVCE YQGQSSDLPQ PPVNAGGGSG - 240
GGSGGGSEGG GSEGGGSEGG GSEGGGSGGG SGSGDFDYEK MANANKGAMT ENADENALQS - 300
DAKGKLDSVA TDYGAAIDGF IGDVSGLANG NGATGDFAGS NSQMAQVGDG DNSPLMNNFR - 360
QYLPSLPQSV ECRPYVFGAG KPYEFSIDCD KINLFRGVFA FLLYVATFMY VFSTFANILR - 420
NKES



Functional narrative    

Plays essential roles both in the entry of the viral genome into the bacterial host and in the budding process. During the initial step of infection, G3P mediates adsorption of the phage to its primary receptor, the tip of host F-pilus. Subsequent interaction with the host coreceptor tolA induces penetration of the viral DNA into the host cytoplasm. In the budding process, G3P mediates the release of the membrane-anchored virion from the cell via its C-terminal domain.

Region 1: 67-90

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name:linker
Location:67 - 90
Length:24
Region sequence:

DETQCYGTWVPIGLAIPENEGGGS

Modification type: Native
PDB: 1G3P:A
Structural/functional type:  
Functional classes:  
Functional subclasses: Flexible linkers/spacers
Detection methods:
  1. X-ray crystallography (100 K; wavelength 0.947 A)

References:
  1. Holliger P, Riechmann L, Williams RL. "Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9 A: evidence for conformational lability." J Mol Biol. 1999; 288(4): 649-57. PubMed: 10329170

  2. Nilsson N, Malmborg AC, Borrebaeck CA. "The phage infection process: a functional role for the distal linker region of bacteriophage protein 3." J Virol. 2000; 74(9): 4229-35. PubMed: 10756036

Comments:
 



References

  1. Nilsson N, Malmborg AC, Borrebaeck CA. "The phage infection process: a functional role for the distal linker region of bacteriophage protein 3." J Virol. 2000; 74(9): 4229-35. PubMed: 10756036



Comments


AV 6-28-2010 PubMed: 10756036


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