Structure-based identification of a novel NTPase from methanococcus jannaschii
- Structure-based identification of a novel NTPase from methanococcus jannaschii
- 황광연; 정지형; 김성호; 한예선; 조윤제
- hyperthetical proteins; nucleotide triphosphatase; functional genomics
- Issue Date
- Nature structural biology
- VOL 6, NO 7, 691-696
- Almost half of the entire set of predicted genomic products from Methanococcus jannaschii are classified as
functionally unknown hypothetical proteins. We present a structure-based identification of the biochemical function
of a protein with an as yet unknown function from a M. jannaschii gene, Mj0226. The crystal structure of Mj0226
protein determined at 2.2 Å resolution reveals that the protein is a homodimer and each monomer folds into an
elongated a/b structure of a new fold family. Comparisons of Mj0226 protein with protein structures in the database,
however, indicate that one part of the protein is homologous to some of the nucleotide-binding proteins. Biochemical
analysis shows that Mj0226 protein is a novel nucleotide triphosphatase that can efficiently hydrolyze nonstandard
nucleotides such as XTP to XMP or ITP to IMP, but not the standard nucleotides, in the presence of Mg2+ or Mn2+ ions.
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