Structural studies of MJ1529, an O6-methylguanine-DNA methyltransferase.
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.
Roberts
Anne
A
Department of Chemistry, University of California and Physical Biosciences Division, Lawrence Berkeley National Lab, Berkeley, CA 94720-1460, USA.
Pelton
Jeffrey G
JG
Wemmer
David E
DE
D000595:Amino Acid Sequence; D017017:Methanococcus / Q000201:enzymology*; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D019853:O(6)-Methylguanine-DNA Methyltransferase / Q000737:chemistry*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
D019853:O(6)-Methylguanine-DNA Methyltransferase