title: Structure-based experimental confirmation of biochemical function to a methyltransferase, MJ0882, from hyperthermophile Methanococcus jannaschii.
abstract: We have determined the three-dimensional (3-D) structure of protein MJ0882, which derives from a hypothetical open reading frame in the genome of the hyperthermophile Methanococcus jannaschii. The 3-D fold of MJ0882 at 1.8 A highly resembles that of a methyltransferase, despite limited sequence similarity to any confirmed methyltransferase. The structure has an S-adenosylmethionine (AdoMet) binding pocket surrounded by motifs with similarities to those commonly found among AdoMet binding proteins. Preliminary biochemical experiments show that MJ0882 specifically binds to AdoMet, which is the essential co-factor for methyltransferases.
authors.affiliation: Dept. of Cellular Biochemistry and Biophysics, Sloan Kettering Institute, 1275 York Ave., New York, NY 10021, USA.
authors.forename: Lan
authors.initials: L
authors.lastname: Huang
authors.forename: Liwei
authors.initials: L
authors.lastname: Hung
authors.forename: Mark
authors.initials: M
authors.lastname: Odell
authors.forename: Hisao
authors.initials: H
authors.lastname: Yokota
authors.forename: Rosalind
authors.initials: R
authors.lastname: Kim
authors.forename: Sung-Hou
authors.initials: SH
authors.lastname: Kim
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000502:physiology; D018360:Crystallography, X-Ray; D017017:Methanococcus / Q000201:enzymology* / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009243:NAD / Q000378:metabolism; D016366:Open Reading Frames; D011485:Protein Binding; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D012435:S-Adenosylhomocysteine / Q000378:metabolism; D012436:S-Adenosylmethionine / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific) / Q000737:chemistry* / Q000502:physiology; D013329:Structure-Activity Relationship
chemical_list: D001426:Bacterial Proteins; D011993:Recombinant Fusion Proteins; D009243:NAD; D012436:S-Adenosylmethionine; D012435:S-Adenosylhomocysteine; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific)