PDBsum entry 2g7h

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protein links
Transferase PDB id
Protein chain
167 a.a. *
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Structure of an o6-methylguanine DNA methyltransferase from methanococcus jannaschii (mj1529)
Structure: Methylated-DNA--protein-cysteine methyltransferase. Chain: a. Synonym: 6-o- methylguanine-DNA methyltransferase, mgmt, o- 6-methylguanine-DNA- alkyltransferase. Engineered: yes
Source: Methanocaldococcus jannaschii. Organism_taxid: 2190. Gene: ogt. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 10 models
Authors: A.Roberts
Key ref: A.Roberts et al. (2006). Structural studies of MJ1529, an O6-methylguanine-DNA methyltransferase. Magn Reson Chem, 44, S71. PubMed id: 16826543
28-Feb-06     Release date:   01-Aug-06    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q58924  (OGT_METJA) -  Methylated-DNA--protein-cysteine methyltransferase
167 a.a.
167 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Methylated-DNA--[protein]-cysteine S-methyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine
DNA (containing 6-O-methylguanine)
+ protein L-cysteine
= DNA (without 6-O-methylguanine)
+ protein S-methyl-L-cysteine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 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     4 terms  


Magn Reson Chem 44:S71 (2006)
PubMed id: 16826543  
Structural studies of MJ1529, an O6-methylguanine-DNA methyltransferase.
A.Roberts, J.G.Pelton, D.E.Wemmer.
The structure of an O6-methylguanine-DNA methyltransferase (MGMT) from the thermophile Methanococcus jannaschii has been determined using multinuclear multidimensional NMR spectroscopy. The structure is similar to homologs from other organisms that have been determined by crystallography, with some variation in the N-terminal domain. The C-terminal domain is more highly conserved in both sequence and structure. Regions of the protein show broadening, reflecting conformational flexibility that is likely related to function.

Literature references that cite this PDB file's key reference

  PubMed id Reference
18803403 Q.Fang, A.M.Noronha, S.P.Murphy, C.J.Wilds, J.L.Tubbs, J.A.Tainer, G.Chowdhury, F.P.Guengerich, and A.E.Pegg (2008).
Repair of O6-G-alkyl-O6-G interstrand cross-links by human O6-alkylguanine-DNA alkyltransferase.
  Biochemistry, 47, 10892-10903.  
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