Structural highlights
Function
[OGT_METJA] Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) in DNA. Repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structural studies of MJ1529, an O6-methylguanine-DNA methyltransferase.,Roberts A, Pelton JG, Wemmer DE Magn Reson Chem. 2006 Jul;44 Spec No:S71-82. PMID:16826543[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Roberts A, Pelton JG, Wemmer DE. Structural studies of MJ1529, an O6-methylguanine-DNA methyltransferase. Magn Reson Chem. 2006 Jul;44 Spec No:S71-82. PMID:16826543 doi:10.1002/mrc.1823
- ↑ Roberts A, Pelton JG, Wemmer DE. Structural studies of MJ1529, an O6-methylguanine-DNA methyltransferase. Magn Reson Chem. 2006 Jul;44 Spec No:S71-82. PMID:16826543 doi:10.1002/mrc.1823
