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Hydrolase PDB id
1pvs
Jmol
Contents
Protein chains
282 a.a. *
Ligands
7HP ×2
Waters ×226
* Residue conservation analysis
PDB id:
1pvs
Name: Hydrolase
Title: 3-methyladenine glcosylase ii(alka) hypoxanthine complex
Structure: DNA-3-methyladenine glycosylase ii. Chain: a, b. Synonym: 3-methyladenine-DNA glycosylase ii, inducible, tag ii, DNA-3-methyladenine glycosidase ii. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Gene: alka or aida or b2068. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.40Å     R-factor:   0.232     R-free:   0.292
Authors: M.Teale
Key ref: M.Teale et al. (2002). 3-methyladenine-DNA glycosylase II: the crystal structure of an AlkA-hypoxanthine complex suggests the possibility of product inhibition. Bioconjug Chem, 13, 403-407. PubMed id: 12009927 DOI: 10.1021/bc015527v
Date:
28-Jun-03     Release date:   08-Jun-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P04395  (3MG2_ECOLI) -  DNA-3-methyladenine glycosylase 2
Seq:
Struc: 		282 a.a.
282 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.2.21  - DNA-3-methyladenine glycosylase Ii.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine, and 7-methyladenine.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     response to DNA damage stimulus   4 terms 
  Biochemical function     catalytic activity     8 terms  

 

 
DOI no: 10.1021/bc015527v Bioconjug Chem 13:403-407 (2002)
PubMed id: 12009927  
 
 
3-methyladenine-DNA glycosylase II: the crystal structure of an AlkA-hypoxanthine complex suggests the possibility of product inhibition.
M.Teale, J.Symersky, L.DeLucas.
 
  ABSTRACT  
 
Escherichia coli (E. coli) protein 3-methyladenine-DNA glycosylase II (AlkA) functions primarily by removing alkylation damage from duplex and single stranded DNA. A crystal structure of AlkA was refined to 2.0 A resolution. This structure in turn was used to refine an AlkA-hypoxanthine (substrate) complex structure to 2.4 A resolution. The complex structure shows hypoxanthine located in AlkA's active site stacked between residues W218 and Y239. The structural analysis of the AlkA and AlkA-hypoxanthine structures indicate that free hypoxanthine binding in the active site may inhibit glycosylase activity.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18472311 G.M.Lingaraju, M.Kartalou, L.B.Meira, and L.D.Samson (2008).
Substrate specificity and sequence-dependent activity of the Saccharomyces cerevisiae 3-methyladenine DNA glycosylase (Mag).
  DNA Repair (Amst), 7, 970-982.  
18464997 L.R.Rutledge, H.F.Durst, and S.D.Wetmore (2008).
Computational comparison of the stacking interactions between the aromatic amino acids and the natural or (cationic) methylated nucleobases.
  Phys Chem Chem Phys, 10, 2801-2812.  
18464978 P.Cysewski (2008).
A post-SCF complete basis set study on the recognition patterns of uracil and cytosine by aromatic and pi-aromatic stacking interactions with amino acid residues.
  Phys Chem Chem Phys, 10, 2636-2645.  
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.