Structure-based identification of a novel NTPase from Methanococcus jannaschii
SCIE
SCOPUS
- Title
- Structure-based identification of a novel NTPase from Methanococcus jannaschii
- Authors
- Hwang, KY; Chung, JH; Kim, SH; Han, YS; Cho, YJ
- Date Issued
- 1999-07
- Publisher
- Nature Publishing Group
- Abstract
- 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 Angstrom, resolution reveals that the protein is a homodimer and each monomer folds into an elongated alpha/beta structure of a new ford 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.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/16309
- DOI
- 10.1038/10745
- ISSN
- 1072-8368
- Article Type
- Article
- Citation
- NATURE STRUCTURAL BIOLOGY, vol. 6, no. 7, page. 691 - 696, 1999-07
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- There are no files associated with this item.
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