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PDBsum entry 3fhf

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protein links
DNA repair, hydrolase, lyase PDB id
3fhf
Jmol
Contents
Protein chain
214 a.a. *
Waters ×153
* Residue conservation analysis
PDB id:
3fhf
Name: DNA repair, hydrolase, lyase
Title: Crystal structure of methanocaldococcus jannaschii 8-oxoguan glycosylase (mjogg)
Structure: N-glycosylase/DNA lyase. Chain: a. Synonym: mjogg. 8-oxoguanine DNA glycosylase. DNA-(apurinic apyrimidinic site) lyase. Ap lyase. Engineered: yes
Source: Methanocaldococcus jannaschii. Organism_taxid: 2190. Gene: 1451601, mj0724, ogg. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.00Å     R-factor:   0.202     R-free:   0.251
Authors: F.Faucher,S.Doublie
Key ref: F.Faucher et al. (2009). Crystal structures of two archaeal 8-oxoguanine DNA glycosylases provide structural insight into guanine/8-oxoguanine distinction. Structure, 17, 703-712. PubMed id: 19446526
Date:
09-Dec-08     Release date:   19-May-09    
PROCHECK
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 Headers
 References

Protein chain
Pfam  
Q58134  (OGG1_METJA) -  N-glycosylase/DNA lyase
Seq:
Struc:
207 a.a.
214 a.a.
Key:    Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.4.2.99.18  - DNA-(apurinic or apyrimidinic site) lyase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   6 terms 
  Biochemical function     catalytic activity     7 terms  

 

 
Structure 17:703-712 (2009)
PubMed id: 19446526  
 
 
Crystal structures of two archaeal 8-oxoguanine DNA glycosylases provide structural insight into guanine/8-oxoguanine distinction.
F.Faucher, S.Duclos, V.Bandaru, S.S.Wallace, S.Doublié.
 
  ABSTRACT  
 
Among the four DNA bases, guanine is particularly vulnerable to oxidative damage and the most common oxidative product, 7,8-dihydro-8-oxoguanine (8-oxoG), is the most prevalent lesion observed in DNA molecules. Fortunately, 8-oxoG is recognized and excised by the 8-oxoguanine DNA glycosylase (Ogg) of the base excision repair pathway. Ogg enzymes are divided into three separate families, namely, Ogg1, Ogg2, and archaeal GO glycosylase (AGOG). To date, structures of members of both Ogg1 and AGOG families are known but no structural information is available for members of Ogg2. Here we describe the first crystal structures of two archaeal Ogg2: Methanocaldococcus janischii Ogg and Sulfolobus solfataricus Ogg. A structural comparison with OGG1 and AGOG suggested that the C-terminal lysine of Ogg2 may play a key role in discriminating between guanine and 8-oxoG. This prediction was substantiated by measuring the glycosylase/lyase activity of a C-terminal deletion mutant of MjaOgg.