spacer
spacer

PDBsum entry 2y1j

Go to PDB code: 
protein dna_rna ligands links
Transferase/DNA PDB id
2y1j

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chain
580 a.a.
DNA/RNA
Ligands
SO4 ×2
Waters ×167
PDB id:
2y1j
Name: Transferase/DNA
Title: Crystal structure of a r-diastereomer analogue of the spore photoproduct in complex with fragment DNA polymerase i from bacillus stearothermophilus
Structure: DNA polymerase i. Chain: a. Fragment: residues 297-876. Engineered: yes. 5'-d( Gp Ap Cp Cp Ap Ap Cp Cp Cp Tp)-3'. Chain: b. Engineered: yes. 5'-d( Ap Gp Gp Gp Qbtp Thm Gp Gp Tp Cp)-3'. Chain: c.
Source: Geobacillus stearothermophilus. Organism_taxid: 1422. Strain: dsm 22. Atcc: 12980. Expressed in: escherichia coli. Expression_system_taxid: 469008. Other_details: german collection of microorganisms (dsm). Synthetic: yes. Synthetic construct.
Resolution:
2.15Å     R-factor:   0.201     R-free:   0.241
Authors: K.Heil,S.Schneider,M.Mueller,A.C.Kneuttinger,T.Carell
Key ref: K.Heil et al. (2011). Crystal structures and repair studies reveal the identity and the base-pairing properties of the UV-induced spore photoproduct DNA lesion. Chemistry, 17, 9651-9657. PubMed id: 21780197
Date:
08-Dec-10     Release date:   27-Jul-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
E1C9K5  (E1C9K5_GEOSE) -  DNA polymerase I from Geobacillus stearothermophilus
Seq:
Struc:
 
Seq:
Struc:
580 a.a.
580 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

DNA/RNA chains
  G-A-C-C-A-A-C-C-C-T 10 bases
  A-G-G-G-QBT-THM-G-G-T-C 10 bases

 Enzyme reactions 
   Enzyme class: 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
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
Chemistry 17:9651-9657 (2011)
PubMed id: 21780197  
 
 
Crystal structures and repair studies reveal the identity and the base-pairing properties of the UV-induced spore photoproduct DNA lesion.
K.Heil, A.C.Kneuttinger, S.Schneider, U.Lischke, T.Carell.
 
  ABSTRACT  
 
UV light is one of the major causes of DNA damage. In spore DNA, due to an unusual packing of the genetic material, a special spore photoproduct lesion (SP lesion) is formed, which is repaired by the enzyme spore photoproduct lyase (Spl), a radical S-adenosylmethionine (SAM) enzyme. We report here the synthesis and DNA incorporation of a DNA SP lesion analogue lacking the phosphodiester backbone. The oligonucleotides were used for repair studies and they were cocrystallized with a polymerase enzyme as a template to clarify the configuration of the SP lesion and to provide information about the base-pairing properties of the lesion. The structural analysis together with repair studies allowed us to clarify the identity of the preferentially repaired lesion diastereoisomer.
 

 

spacer

spacer