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PDBsum entry 2fio

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protein dna_rna Protein-protein interface(s) links
Transcription/DNA PDB id
2fio

 

 

 

 

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Contents
Protein chains
123 a.a.
113 a.a.
DNA/RNA
Waters ×86
PDB id:
2fio
Name: Transcription/DNA
Title: Phage phi29 transcription regulator p4-DNA complex
Structure: DNA (41-mer). Chain: c. Engineered: yes. DNA (41-mer). Chain: d. Engineered: yes. Late genes activator. Chain: a, b. Synonym: early protein gp4.
Source: Synthetic: yes. Bacillus phage phi29. Organism_taxid: 10756. Gene: 4. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Tetramer (from PQS)
Resolution:
2.70Å     R-factor:   0.229     R-free:   0.279
Authors: D.Badia,A.Camacho,L.Perez-Lago,C.Escandon,M.Salas,M.Coll
Key ref:
D.Badia et al. (2006). The structure of phage phi29 transcription regulator p4-DNA complex reveals an N-hook motif for DNA. Mol Cell, 22, 73-81. PubMed id: 16600871 DOI: 10.1016/j.molcel.2006.02.019
Date:
30-Dec-05     Release date:   26-Sep-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
P03682  (TF4_BPPH2) -  Late genes activator p4 from Bacillus phage phi29
Seq:
Struc:
125 a.a.
123 a.a.
Protein chain
P03682  (TF4_BPPH2) -  Late genes activator p4 from Bacillus phage phi29
Seq:
Struc:
125 a.a.
113 a.a.
Key:    Secondary structure  CATH domain

DNA/RNA chains
  A-A-A-A-A-C-G-T-C-A-A-C-A-T-T-T-T-A-T-A-A-A-A-A-A-G-T-C-T-T-G-C-A-A-A-A-A-G-T- 41 bases
  T-A-A-C-T-T-T-T-T-G-C-A-A-G-A-C-T-T-T-T-T-T-A-T-A-A-A-A-T-G-T-T-G-A-C-G-T-T-T- 41 bases

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1016/j.molcel.2006.02.019 Mol Cell 22:73-81 (2006)
PubMed id: 16600871  
 
 
The structure of phage phi29 transcription regulator p4-DNA complex reveals an N-hook motif for DNA.
D.Badia, A.Camacho, L.Pérez-Lago, C.Escandón, M.Salas, M.Coll.
 
  ABSTRACT  
 
Protein p4 affects the transcriptional switch that divides bacteriophage phi29 infection in early and late phases. The synthesis of DNA replication proteins and p4 takes place in the early phase, while structural, morphogenesis, and lysis proteins are synthesized in the late phase. Transcriptional switch by p4 is achieved by activating the late promoter A3 and repressing the early promoters A2b and A2c. The crystal structure of p4 alone and in complex with a 41 bp DNA, including the A3 promoter binding site, helps us to understand how the phage cycle is controlled. Protein p4 has a unique alpha/beta fold that includes a DNA recognition motif consisting of two N-terminal beta turn substructures, or N-hooks, located at the tips of an elongated protein homodimer. The two N-hooks enter the major groove of the double helix, establishing base-specific contacts. A high DNA curvature allows p4 N-hooks to reach two major groove areas three helical turns apart, like a bow and its string.
 
  Selected figure(s)  
 
Figure 2.
Figure 2. Structure of the p4 Monomer and the N-Hook
Figure 3.
Figure 3. Structure of the p4 Dimer-DNA Complex
 
  The above figures are reprinted by permission from Cell Press: Mol Cell (2006, 22, 73-81) copyright 2006.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20334529 R.Rohs, X.Jin, S.M.West, R.Joshi, B.Honig, and R.S.Mann (2010).
Origins of specificity in protein-DNA recognition.
  Annu Rev Biochem, 79, 233-269.  
18957612 K.Porter, B.E.Russ, J.Yang, and M.L.Dyall-Smith (2008).
The transcription programme of the protein-primed halovirus SH1.
  Microbiology, 154, 3599-3608.  
17452358 J.Mendieta, L.Pérez-Lago, M.Salas, and A.Camacho (2007).
DNA sequence-specific recognition by a transcriptional regulator requires indirect readout of A-tracts.
  Nucleic Acids Res, 35, 3252-3261.  
17441785 M.Salas, and M.Salas (2007).
40 years with bacteriophage ø29.
  Annu Rev Microbiol, 61, 1.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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