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PDBsum entry 3oye

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protein dna_rna ligands metals Protein-protein interface(s) links
Recombination,viral protein/DNA PDB id
3oye

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
368 a.a. *
184 a.a. *
DNA/RNA
Ligands
SO4 ×2
GOL ×4
NH4
ZYY
Metals
_MG ×3
_ZN
Waters ×217
* Residue conservation analysis
PDB id:
3oye
Name: Recombination,viral protein/DNA
Title: Crystal structure of the prototype foamy virus (pfv) intasome in complex with magnesium and the insti compound2
Structure: Pfv integrase. Chain: a, b. Fragment: unp residues 752 to 1143. Synonym: p42in. Engineered: yes. DNA (5'- d( Ap Tp Tp Gp Tp Cp Ap Tp Gp Gp Ap Ap Tp Tp Tp Cp Gp Cp A)-3'). Chain: c. Engineered: yes.
Source: Human spumaretrovirus. Sfvcpz(hu). Organism_taxid: 11963. Strain: hsrv2. Gene: pol. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: donor DNA non-transferred strand.
Resolution:
2.74Å     R-factor:   0.205     R-free:   0.234
Authors: S.Hare,P.Cherepanov
Key ref: S.Hare et al. (2010). Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance. Proc Natl Acad Sci U S A, 107, 20057-20062. PubMed id: 21030679
Date:
23-Sep-10     Release date:   17-Nov-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P14350  (POL_FOAMV) -  Pro-Pol polyprotein from Human spumaretrovirus
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1143 a.a.
368 a.a.*
Protein chain
Pfam   ArchSchema ?
P14350  (POL_FOAMV) -  Pro-Pol polyprotein from Human spumaretrovirus
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1143 a.a.
184 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

DNA/RNA chains
  A-T-T-G-T-C-A-T-G-G-A-A-T-T-T-C-G-C-A 19 bases
  T-G-C-G-A-A-A-T-T-C-C-A-T-G-A-C-A 17 bases

 Enzyme reactions 
   Enzyme class 2: Chains A, B: E.C.2.7.7.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 3: Chains A, B: E.C.2.7.7.49  - RNA-directed Dna polymerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate
DNA(n)
+ 2'-deoxyribonucleoside 5'-triphosphate
= DNA(n+1)
+ diphosphate
   Enzyme class 4: Chains A, B: E.C.2.7.7.7  - DNA-directed Dna polymerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate
DNA(n)
+ 2'-deoxyribonucleoside 5'-triphosphate
= DNA(n+1)
+ diphosphate
   Enzyme class 5: Chains A, B: E.C.3.1.-.-
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 6: Chains A, B: E.C.3.1.26.4  - ribonuclease H.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endonucleolytic cleavage to 5'-phosphomonoester.
   Enzyme class 7: Chains A, B: E.C.3.4.23.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Proc Natl Acad Sci U S A 107:20057-20062 (2010)
PubMed id: 21030679  
 
 
Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance.
S.Hare, A.M.Vos, R.F.Clayton, J.W.Thuring, M.D.Cummings, P.Cherepanov.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21277766 P.Cherepanov, G.N.Maertens, and S.Hare (2011).
Structural insights into the retroviral DNA integration apparatus.
  Curr Opin Struct Biol, 21, 249-256.  
21493066 X.Z.Zhao, K.Maddali, M.Metifiot, S.J.Smith, B.C.Vu, C.Marchand, S.H.Hughes, Y.Pommier, and T.R.Burke (2011).
Development of tricyclic hydroxy-1H-pyrrolopyridine-trione containing HIV-1 integrase inhibitors.
  Bioorg Med Chem Lett, 21, 2986-2990.  
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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