title: Structural studies of MJ1529, an O6-methylguanine-DNA methyltransferase.
abstract: 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.
authors.affiliation: Department of Chemistry, University of California and Physical Biosciences Division, Lawrence Berkeley National Lab, Berkeley, CA 94720-1460, USA.
authors.forename: Anne
authors.initials: A
authors.lastname: Roberts
authors.forename: Jeffrey G
authors.initials: JG
authors.lastname: Pelton
authors.forename: David E
authors.initials: DE
authors.lastname: Wemmer
mesh_terms: 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
chemical_list: D019853:O(6)-Methylguanine-DNA Methyltransferase