Hwang, KY Chung, JH Kim, SH Han, YS Cho, YJ 2024-01-21T15:15:41Z 2024-01-21T15:15:41Z 2021-09-04 1999-07 1072-8368 https://pubs.kist.re.kr/handle/201004/142109 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. English NATURE AMERICA INC COMPLETE GENOME SEQUENCE TRANSFER-RNA SYNTHETASE CRYSTAL-STRUCTURE ESCHERICHIA-COLI SACCHAROMYCES-CEREVISIAE THERMUS-THERMOPHILUS PROTEIN DATABASE 6-N-HYDROXYLAMINOPURINE RESOLUTION Structure-based identification of a novel NTPase from Methanococcus jannaschii Article 1 NATURE STRUCTURAL BIOLOGY, v.6, no.7, pp.691 - 696 NATURE STRUCTURAL BIOLOGY 6 7 691 696 scie scopus 000081217500025 2-s2.0-17444398048 Biochemistry & Molecular Biology Biophysics Cell Biology Biochemistry & Molecular Biology Biophysics Cell Biology Article COMPLETE GENOME SEQUENCE TRANSFER-RNA SYNTHETASE CRYSTAL-STRUCTURE ESCHERICHIA-COLI SACCHAROMYCES-CEREVISIAE THERMUS-THERMOPHILUS PROTEIN DATABASE 6-N-HYDROXYLAMINOPURINE RESOLUTION hyperthetical proteins nucleotide triphosphatase functional genomics