2mjp

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spinqualitylabelsall models 2mjp, resolution 2.2Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE-BASED IDENTIFICATION OF THE BIOCHEMICAL FUNCTION OF A HYPOTHETICAL PROTEIN FROM METHANOCOCCUS JANNASCHII:MJ0226

Overview

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 A resolution reveals that the protein is a homodimer and, each monomer folds into an elongated alpha/beta 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.

About this Structure

2MJP is a Single protein structure of sequence from Methanocaldococcus jannaschii with ANP as ligand. Full crystallographic information is available from OCA.

Reference

Structure-based identification of a novel NTPase from Methanococcus jannaschii., Hwang KY, Chung JH, Kim SH, Han YS, Cho Y, Nat Struct Biol. 1999 Jul;6(7):691-6. PMID:10404228

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