1mjh

File:1mjh.gif

spinqualitylabelsall models 1mjh, resolution 1.7Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE-BASED ASSIGNMENT OF THE BIOCHEMICAL FUNCTION OF HYPOTHETICAL PROTEIN MJ0577: A TEST CASE OF STRUCTURAL GENOMICS

OverviewOverview

Many small bacterial, archaebacterial, and eukaryotic genomes have been, sequenced, and the larger eukaryotic genomes are predicted to be, completely sequenced within the next decade. In all genomes sequenced to, date, a large portion of these organisms' predicted protein coding regions, encode polypeptides of unknown biochemical, biophysical, and/or cellular, functions. Three-dimensional structures of these proteins may suggest, biochemical or biophysical functions. Here we report the crystal structure, of one such protein, MJ0577, from a hyperthermophile, Methanococcus, jannaschii, at 1.7-A resolution. The structure contains a bound ATP, suggesting MJ0577 is an ATPase or an ATP-mediated molecular switch, which, we confirm by biochemical experiments. Furthermore, the structure reveals, different ATP binding motifs that are shared among many homologous, hypothetical proteins in this family. This result indicates that, structure-based assignment of molecular function is a viable approach for, the large-scale biochemical assignment of proteins and for discovering new, motifs, a basic premise of structural genomics.

About this StructureAbout this Structure

1MJH is a Single protein structure of sequence from Methanocaldococcus jannaschii with MN and ATP as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Structure-based assignment of the biochemical function of a hypothetical protein: a test case of structural genomics., Zarembinski TI, Hung LW, Mueller-Dieckmann HJ, Kim KK, Yokota H, Kim R, Kim SH, Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15189-93. PMID:9860944

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